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Arthritis and inflammatory eye disease

Arthritis and inflammatory eye disease

The rheumatologist ignores the association between connective tissues diseases and the eye at his or her peril. Failure to recognize the significance of temporal headaches indicative of temporal arteritis in patients with polymyalgia rheumatic may result in acute loss of vision with blindness. In contrast, visual symptoms may only present when irreversible damage to the eye has occurred, as in the case of the insidious onset of intermediate uveitis in children with pauci-articular JCA with a positive ANA.

Abnormal connective tissue components such as collagen or fibrillin (in the case of Marfan’s syndrome) may lead to different forms of arthropathy and visual loss depending on the type of collagen in the tissues involved. For example, defective synthesis of type I collagen leads to osteoporosis and blue sclera in osteogenesis imperfecta. In the very rare condition of osteoporosis–pseudoglioma syndrome, where there is a mutation in the low-density lipoprotein receptor-related protein 5 (LRP5), there is an association between reduced bone mass, resulting in osteoporosis, and a defect in vitreal macrophage function with vitreal vessel regression, resulting in blindness .Patients with Stickler’s syndrome, who have a defect in the synthesis of type II A collagen, present with premature osteoarthritis requiring early joint replacement, and loss of vision due to defects in the synthesis of collagen in the vitreus, resulting in retinal detachment .Defects in the synthesis of type II B collagen results in arthrogryposis and keratoconus, in which visual loss is due to changes in physical properties of the cornea.

Similarly, inflammatory disorders of the eye may be associated with different connective tissue disorders. There may be a strong association with particular genes but the phenotypic presentation may depend on the anatomical site of the ocular lesion. The classical example of this is the unilateral acute onset of anterior uveitis in patients with ankylosing spondylitis and other seronegative arthritides, associated with a high frequency of HLA B27. Each acute attack usually responds to local steroid drops and mydriatics and if promptly treated does not result in any residual damage to the eye. Genetic variations in proinflammatory mediators and their receptors appear to influence the susceptibility and severity of the inflammatory response within the eyes of patients prone to development of idiopathic acute anterior uveitis.

Intermediate uveitis involves the anterior and posterior (pars plana) ciliary body, the former affected sometimes in patients with sarcoidosis, and the latter, presenting with pars planitis, may be associated with multiple sclerosis (MS).

The posterior uveal tract may be involved in patients with a number of systemic diseases, including Behçet’s syndrome. This is a polygenic disease and although no clear pattern of inheritance has been established, the most closely associated risk factor is HLA B5. It is of interest that chromosome 6 contains the HLA B5 locus and in close proximity to it are several other genes related to inflammation, including tumour necrosis factor (TNF). The TNF inhibitor infliximab has demonstrated great promise in the treatment of Behçet’s disease. In Behçet’s syndrome there is not only an inflammatory process but also a thrombotic risk, possibly related to the presence of factor V Leiden. Recently a study has shown that 44% of patients with retinal occlusive disease have the factor V Leiden mutation .The Vogt–Koyanagi–Harada (VKH) syndrome is a multisystem disease characterized by acute bilateral panuveitis. Patients may present with a polyarthritis but the organs that contain melanocytes are targets of inflammation, resulting in areas of depigmentation in the skin and eyebrows (poliosis). Involvement of the central nervous system with sterile meningitis and the inner ears may also be affected. Involvement of the uveal tract results in retinal detachment. VKH is considered to be an autoinflammatory disease against melanocyte antigens .VKH, like rheumatoid arthritis, is associated with HLA DR4 but the implicated HLA DR4 subtypes differ for the two diseases. Evidence suggests that a defective Fas-mediated apoptosis response is found in lymphocytes of VKH and Behçet’s disease patients .

Recently there has been great interest in an autosomal dominantly inherited triad of granulomatous inflammation in the uveal tract, skin and joints in a condition called familial juvenile systemic granulomatosis or Blau syndrome .Mutations in the Nod 2/Card 15 genes were reported to be associated with familial juvenile systemic granulomatosis in four families and different mutations of the same gene are associated with Crohn’s disease. Patients with Blau syndrome present with features consistent with Crohn’s disease. The Nod 2/Card 15 gene encodes an intracellular protein that is thought to be involved in sensing intracellular bacteria and participates in important signalling cascades leading to NF-κB activation and possibly apoptosis .Nod 2 proteins specifically detect the muramyl dipeptide component of peptidoglycan, a cell wall constituent of both Gram-positive and Gram-negative bacteria . It is suggested that Nod 2 may be expressed not only in the inflammatory cells migrating to tissues (i.e. monocytes, macrophages) but also in the tissues themselves, especially cell types that are involved in gatekeeper functions during the process of inflammation with respect to the intestinal epithelium and vascular endothelium .

Rheumatoid arthritis is associated with scleritis, scleromalacia perforans and corneal melt. Traditionally it was assumed that the cornea was an immunologically privileged site due to paucity of blood vessels and lymphatics. However, it is now thought that immune cells may in fact pass between the eye and the systemic vascular and lymphatic circulations but, through a process of apoptosis, become inactivated. Griffith and colleagues .demonstrated that the apoptosis-inducing cell membrane molecule Fas ligand is expressed on multiple ocular cells, including the corneal epithelium and endothelium. Inflammatory cells such as neutrophils and activated T cells are especially vulnerable to apoptosis induced by Fas ligand expressed on ocular cells. Approximately 50% of the corneal grafts from donor mouse strains that expressed functional Fas ligand on the corneal epithelium and endothelium, experienced long-term survival. By contrast, rejection occurred in 89–100% of the corneal grafts prepared from mutant mice that failed to express functional Fas ligand. Thus, Fas ligand creates a functional blockade of the efferent arm of the immune response.

As far as the uveal tract is concerned, there are two animal models that may have relevance to uveitis seen in the human. Endotoxin-induced uveitis was described by Rosenbaum et al. who showed that injection of lipopolysaccharide into the footpad of rats induced an acute anterior uveitis, the cellular infiltrate being mainly neutrophils. In experimental autoimmune uveoretinitis retinal antigens were injected into rats. The inflammation occurred in the posterior uveal tract and the dominant cell type was a CD4 lymphocyte.

The treatment of inflammatory eye disease is at present somewhat controversial. With respect to peripheral ulcerative keratitis (corneal melt), the treatment of choice would appear to be cyclophosphamide given intravenously, on the basis that this probably represents a form of vasculitis .

The use of TNF-α-blocking therapy in the treatment of uveitis is at present a controversial area In a recent trial of infliximab therapy in refractory uveitis, of 31 enrolled subjects 28 reached 10 weeks in the study. At the initial end-point for assessing efficacy, 18 reached 1 yr and five reached the 2-yr end-point. At these time points 22/28, 9/18 and 1/5 were characterized by treatment successes. However, there was a high frequency of adverse events, with three cases of drug-induced lupus, one neoplasm, three thromboembolic side-effects, one case of congestive heart failure and one infectious complication. Thirteen of the 18 patients who reached 1 yr of the study developed positive ANA, but this did not correlate with treatment efficacy or toxicity. Several published observations have suggested that etanercept, in spite of its efficacy in treating arthritis, may actually induce attacks of uveitis in patients who have not previously experienced such episodes. In a retrospective study of 16 patients with a variety of inflammatory eye and joint diseases, there was a universal benefit from TNF inhibition for the joint disease, but only a 38% response rate for the associated uveitis or scleritis, and in five patients ocular inflammation began only after etanercept therapy was started. However, Rosenbaum reported that three randomized studies on the effect of etanercept for ankylosing spondylitis provided reassuring data. However, more recently a report has indicated that in the context of juvenile chronic arthritis the use of etanercept was associated with an increase in relapse rates and first attacks of uveitis in children treated with it]. In a case report by Taban, a patient treated with etanercept for ankylosing spondylitis and bilateral anterior uveitis exhibited acute exacerbation of uveitis that were temporally related to etanercept injections .A recent report of 18 patients treated with anti-TNF therapy using both infliximab and etanercept showed that 13 out of 15 patients treated with infliximab had either complete or partial control of ocular inflammation, whereas all seven patients treated with etanercept failed therapy and five of these were changed to infliximab therapy; four of these achieved either complete or partial response after initiation of infliximab treatment .

In conclusion the jury is still out regarding the benefits and toxicity of different TNF-α-blockers in relation to inflammatory eye disease. It is of interest that in the endotoxin-induced uveitis model, mice treated with TNF-α antibody demonstrated an exacerbation of uveitis .Furthermore, the inflammation proceeded despite the genetic deletion of TNF-α receptors . This probably represents a neutrophil-mediated inflammatory process in comparison with the favourable effect of TNF inhibition in a T-cell mediated model of uveitis .The differential effects of infliximab versus etanercept may lie in the fact that infliximab induces cell lysis after binding to TNF-α and induces apoptosis of T lymphocytes .whereas etanercept neutralizes lymphotoxin-α. This may explain why infliximab and not etanercept is beneficial in the treatment of Crohn’s disease, but in the case of arthritis in JCA etanercept may be the drug of choice.

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How To Choose A Good Medical Research Paper Topic

How To Choose A Good Medical Research Paper Topic:

We are living much healthier life, thanks to tremendous research, advances and breakthroughs in the field of medical science regarding treatment of hundreds of formerly incurable diseases. Medical science, no doubt, is a special type of blessing for human beings. Writing a research paper on any topic is not easy by any means and it becomes even tougher when it comes to writing on a medical research paper topic. Because, medical science is different field and it has its own specific terminologies. You are required only to write scientific facts with the help of biological terminologies for your medical research paper.

You cannot write your detailed views, unlike writing a research paper on poverty, while working on a medical research paper. You must be precise, artistic, calculated and scientific in your approach to dealing with your topic properly. It is, therefore, more important to choose a good and an easy topic for your research paper. You must be aware of all pros and cons of your topic along with having the latest and sufficient of current research in that field.

How To Choose Medical Research Paper Topics

You should choose a topic that would keep you interested. There are hundreds of topics regarding medical science. You can choose any of the topics that would be easy for you to work on. But, if you do not have natural inclinations towards any of them, you can ask your teacher to give you an interesting topic or you can also consult internet for this purpose. Once you have chosen the right topic for your research paper, it would be much easier to work on it. You can find current relevant knowledge from the internet, by consulting medical journals and from medical libraries.

Some Of The Proposed Medical Research Paper Topics

You can write Down Syndrome Research Paper, Breast Cancer Research Paper, Alzheimer’s disease research paper, AIDS research paper, Hepatitis research paper, Euthanasia Research Paper, Swine flu research paper, Diabetes Research Paper etc.

How To Work On A Medical Research Paper Topic

Give an introduction by defining your medical research paper topic. There should be main body of your research paper right after the introduction in which you should elaborate on the causes and effects of a disease, disorder or a medical issue relating to your specific topic. In this part, you must write with the help of correct data to describe its details. In the end, sum up your topic with most likely arguments, assumption or proposals according to your specific topic.

Some Useful Tips

• Choose a topic that is easy and according to your natural interests.

• Medical terminologies are quite difficult, so, try to keep your research paper as simple as possible by giving most of the details in common but interesting style.

• You must use correct and latest information by quoting your references correctly.

• Try to discuss your topic in a unique style.

• Read your paper after completion to avoid mistakes.

Diabetes Research Paper

Simple Way Of Writing Diabetes Research Papers

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The Differences between viral pneumonia and bacterial pneumonia

What is pneumonia ?

Pneumonia can be caused by different types of infections such as bacterial, viral, fungal and even parasitic infections. The most common causes of pneumonia include bacterial and viral infections. The pathophysiology of pneumonia in both cases is somewhat similar. But there are a few differences between viral and bacterial pneumonia. The following paragraphs on viral vs. bacterial pneumonia will help clear out the differences between the two and help you find the causative agent of this respiratory ailment.

The Differences between viral pneumonia and bacterial pneumonia:
In many cases, parents are often confused as they do not seem to understand if their child is showing signs of bacterial or viral pneumonia. We shall have a look at both the infections separately that will help lay some doubts to rest and distinguish between the two of them.

What is Bacterial Pneumonia?

Bacterial pneumonia is generally caused by Streptococcus pneumoniae. It commonly affects people with a weak immune system like those over the age of 65 years, immunocompromised individuals with HIV/AIDS, people with diabetes, heart ailments, lung diseases, etc. Staphylococcus aureus and Streptococcus agalactiae are known to cause pneumonia in newborn babies. Other bacteria capable of causing pneumonia include Escherichia coli, Klebsiella pneumoniae, Haemophilus influenzae, Pseudomonas aeruginosa and Moraxella catarrhalis. The bacteria enter the body through inhalation of airborne droplets. These bacteria tend to live in the upper respiratory tract and can be inhaled into the lungs. When the bacteria enters the lungs, it triggers an immune response. The neutrophils reach the lungs and engulf the bacterial agents. While doing so, these cells release cytokines that trigger activation of the entire immune system. This leads to many bacterial pneumonia symptoms that include -Chills
Cough with greenish mucus
Chest pain,
In severe cases, one will observe a blue tint under the nails and on the lips. Lethargy, drowsiness and the blue tint are seen because the neutrophils, bacteria and the fluid from the blood vessels fill up the alveolar sacs. This causes disruption of normal oxygen transportation leading to these symptoms. The treatment for bacterial pneumonia includes use of antibiotics like penicillin. In severe cases, the person is hospitalized and given oxygen therapy along with intravenous fluids. Analgesics and acetaminophen are given to reduce chest pain and fever.

What is Viral Pneumonia?

Most of the cases of pneumonia are caused due to a viral infection. The viruses that cause pneumonia are influenza virus, respiratory syncytial virus (RSV), adenovirus and parainfluenza virus. Pneumonia in newborns can be caused by herpes simplex virus in rare occasions. The viral agents reach the lungs through inhalation via the mouth and nose. After entering the lungs, the virus reaches the cells of the airways and alveoli. The viral invasion causes cell death and the immune system begins to act against the invading organism. The lymphocytes activate cytokines that cause fluid build up in alveoli. A person suffering from viral pneumonia shows the following symptoms –
Dry cough that will progress to wet cough
Sore throat
Loss of appetite
Muscle pain
Shortness of breath

The fluid build up in the alveoli decreases oxygen transportation to the blood. This leads to extreme breathlessness and blue tint of the lips and under the nails. Viral pneumonia is a less severe infection than bacterial pneumonia. Antibiotics and antibacterial drugs will not help in treatment of viral pneumonia. The patient is given antibiotics only if there are chances of secondary bacterial infection. Viral pneumonia is treated by giving the patient plenty of rest and warm fluids to drink. Antiviral drugs like zanamivir or amantadine may be prescribed.

From the above explanations, it becomes easy to differentiate between viral vs. bacterial pneumonia. Bacterial pneumonia symptoms are more severe than viral pneumonia. The symptoms of viral pneumonia develop gradually over a couple of days while bacterial pneumonia tends to develop rapid symptoms. Hope the above information has helped you understand the difference between viral and bacterial pneumonia better.

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A biosensor is an analytical device, used for the detection of an analyte , that combines a biological component with a physicochemical detector

A common example of a commercial biosensor is the blood glucose biosensor, which uses the enzyme glucose oxidase to break blood glucose down.

A device that detects, records, and transmits information regarding a physiological change or process.

a sensor device for detecting and measuring very small quantities or changes in a biochemical or chemical substance, in which a microelectronic component registers reactions related to the substance and translates them into data

There are different types of business based on different principles. However, generally they are categorized as:
According to the mode of interaction business are of two types:
Catalytic biosensor: The interaction of biological material in the biosensor and the annually result in modification of annually into new chemical molecule. The biological material used is mainly enzymes.
Affinity biosensor: Here, upon interaction, the analyte binds to the biomolecule on the biosensor. These are mainly composed of antibodies, nucleic acids etc.

Essential properties of a biosensor:
(i) Specificity: a biosensor should be specific to the analyte which it interact.
(ii) Durability: it should withstand repeated usage.
(iii) Independent nature: It should not be affected by variations in the environment like temperature, pH etc.
(iv) Stability in results: the results produced by interaction should be corresponding to the concentration of analyte.
(v) Ease of use and transport: it should be small in size so that it can be easily carried and used.

Components and mechanism of a biosensor:
A biosensor mainly consists of two parts
(i) a biological part: this constitutes of enzymes antibodies etc., which mainly interacts with the analyte particles and induce a physical change in these particles.
(ii) a transducer part: which collects information from the biological part, converts, amplifies and display them. In order to form a biosensor, the biological particles are immobilized on the transducer surface which acts as a point of contact between the transducer and analyte.
When a biosensor is used to analyse a sample, the biological part specific to the analyte molecules, interacts specifically and efficiently. This produces a physicochemical change of the transducer surface. This change is picked up by the transducer and gets converted into electric signals. These then undergo amplification, interpretation and finally display of these electric units accounting to the amount of analyte present in the sample.

Types of biosensors:
(i) Calorimetric biosensor: some enzyme- analyte reactions are exothermic and releases heat into the sample. This change in temperature is detected by the transducer. The amount of heat generated is proportional to the analyte concentration present and is processed likewise.
(ii) Potentiometric biosensor: an electric potential is produced as a result of interaction which is detected by the transducer
(iii) Amperometric biosensor: analyte when comes in contact with biological material induces a redox reaction. This results in movement of electrons which is picked up by transducer.
(iv) Optical biosensors: in this, a biosensor reacts with analyte to absorb or release light which is identified by the transducer and interpreted.
(v) Acoustic wave biosensors: biological component of biosensor undergoes a biomass change ascertained by transducer.
The advantages of biosensors include accuracy in results, minute detection capability, ease of use, versatile and continuous monitoring available.
A biosensor has a wide range of applications in different fields.
Medicinal Application: biosensors have been used in various diagnostic procedures to determine various tests.
Industrial application: various manufacturing processes can be monitored by biosensors to provide assistance with regard to increase the quality and quantity of product obtained.
Environmental application: it helps in measuring the toxicity of water bodies, microbial contamination of natural resources helping in developing steps towards a cleaner environment.
Military application: it helps to detect explosives, drugs etc., aiding in defence of the people. Another breakthrough in the field of biosensors was the production of a product called ‘smart skin’. It is a kind of biosensor which detects any chemical or biological attack nearby and warns the person using the same.
Drug development: a biosensor called ‘nano sensors’ has been developed which detects and analyse the binding of proteins to its targets which has proved very useful in drug designing. This also helps to monitor certain side effects caused by some medicines.


Bioadhesives are natural polymeric materials that act as adhesives. The term is sometimes used more loosely to describe a glue formed synthetically from biological monomers such as sugars, or to mean a synthetic material designed to adhere to biological tissue. …Source or sample of word “bioadhesive”

Bioadhesives are natural polymeric materials that act as adhesives. The term is sometimes used more loosely to describe a glue formed synthetically from biological monomers such as sugars, or to mean a synthetic material designed to adhere to biological tissue.

Bioadhesives may consist of a variety of substances, but proteins and carbohydrates feature prominently. Proteins such as gelatin and carbohydrates such as starch have been used as general-purpose glues by man for many years

Examples of bioadhesives in nature

Organisms may secrete bioadhesives for use in attachment, construction and obstruction, as well as in predation and defense. Examples[2] include their use for

  • colonization of surfaces (e.g. bacteria, algae, fungi, mussels, barnacles)
  • tube building by polychaete worms, which live in underwater mounds
  • insect egg, larval or pupal attachment[3] to surfaces (vegetation, rocks), and insect mating plugs
  • host attachment by blood-feeding ticks
  • nest-building by some insects, and also by some fish (e.g. the three-spined stickleback)
  • defense by Notaden frogs and by sea cucumbers
  • prey capture in spider webs and by velvet worms

Commercial applications

Shellac is an early example of a bioadhesive put to practical use. Additional examples now exist, with others in development:

  • Commodity wood adhesive based on a bacterial exopolysaccharide[7]
  • USB PRF/Soy 2000, a commodity wood adhesive that is 50% soy hydrolysate and excels at finger-jointing green lumber[8]
  • Mussel adhesive proteins can assist in attaching cells to plastic surfaces in laboratory cell and tissue culture experiments (see External Links)
  • The Notaden frog glue is under development for biomedical uses, e.g. as a surgical glue for orthopedic applications or as a hemostat[9]
  • Mucosal drug delivery applications. For example, films of mussel adhesive protein give comparable mucoadhesion to polycarbophil,[10] a synthetic hydrogel used to achieve effective drug delivery at low drug doses. An increased residence time through adhesion to the mucosal surface, such as in the eye or the nose can lead to an improved absorption of the drug.[11]

Several commercial methods of production are being researched:

  • direct chemical synthesis, e.g. incorporation of L-DOPA groups in synthetic polymers[12]
  • fermentation of transgenic bacteria or yeasts that express bioadhesive protein genes
  • farming of natural organisms (small and large) that secrete bioadhesive materials


Iontophoresis, also called electromotive drug administration (EMDA), is a technique using a small electric charge to deliver a medicine or other chemical through the skin It is basically an injection without the needle. The technical description of this process is a non-invasive method of propelling high concentrations of a charged substance, normally a medication or bioactive agent, transdermally by repulsive electromotive force using a small electrical charge applied to an iontophoretic chamber containing a similarly charged active agent and its vehicle. One or two chambers are filled with a solution containing an active ingredient and its solvent, also called the vehicle. The positively charged chamber, called the anode, will repel a positively charged chemical, whereas the negatively charged chamber, called the cathode, will repel a negatively charged chemical into the skin.

the motion of charged particles in a colloid under the influence of an electric field; particles with a positive charge go to the cathode and negative to the anode.

Ionophoresis is a type of:
  • natural process, natural action, action, activity (noun) – a process existing in or produced by nature (rather than by the intent of human beings)

Types of ionophoresis:

  • immunoelectrophoresis (noun) – electrophoresis to separate antigens and antibodies
  • paper electrophoresis, carrier electrophoresis (noun) – electrophoresis carried out on filter paper

ionophoresis is derivationally related to:

  • electrophoretic, cataphoretic (adjective) – of or relating to electrophoresis

Iontophoresis is well classified for use in transdermal drug delivery. Unlike transdermal patches, this method relies on active transportation within an electric field. In the presence of an electric field electromigration and electroosmosis are the dominant forces in mass transport. These movements are measured in units of chemical flux, commonly µmol/cm2h.

Reverse iontophoresis is the process by which molecules are removed from within the body for detection. In reverse iontophoresis, the negative charge of the skin at buffered pH causes it to be permselective to cations, causing solvent flow towards the anode. This flow is the dominant force, allowing movement of neutral molecules, including glucose, across the skin. This technology is currently being used in such devices as the GlucoWatch, which allows for blood glucose detection across skin layers using reverse iontophoresis.

Iontophoresis is commonly used by physical therapists for the application of anti-inflammatory medications. Common diagnoses treated with Iontophoresis include plantar fasciitis, bursitis, and some types of hyperhidrosis. In this specific application, the solution chosen is usually tap water, but better results can be obtained using glycopyrronium bromide, a cholinergic inhibitor. Iontophoresis of acetylcholine is used in research as a way to test the health of the endothelium by stimulating endothelium-dependent generation of nitric oxide and subsequent microvascular vasodilation. Acetylcholine is positively charged and, therefore, placed in the anode.

Pilocarpine iontophoresis is often used to stimulate sweat secretion, as part of cystic fibrosis diagnosis

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The Chemical Reaction classification

Chemical Reaction,Types of Chemical Reaction,Classification of Chemical Reaction

What Are Types of Chemical Reactions?

The Chemical reactions involve the motion of electrons, leading to the formation and breaking of chemical bonds. There are several different types of chemical reactions.

Some common reaction types are:

Direct Combination or Synthesis Reaction

In a synthesis reaction two or more chemical species combine to form a more complex product.

The combination of iron and sulfur to form iron (II) sulfide is an example of a synthesis reaction:

8 Fe + S8 –> 8 Fe S

Chemical Decomposition or Analysis Reaction

In a decomposition reaction a compound is broken into smaller chemical species.

The electrolysis of water into oxygen and hydrogen gas is an example of a decomposition reaction:

2 H2O –> 2 H2 + O2

Single Displacement or Substitution Reaction

A substitution or single displacement reaction is characterized by one element being displaced from a compound by another element.

An example of a substitution reaction occurs when zinc combines with hydrochloric acid. The zinc replaces the hydrogen:

Zn + 2 H Cl –> ZnCl2 + H2

Metathesis or Double Displacement Reaction

In a double displacement or metathesis reaction two compounds exchange bonds or ions in order to form different compounds.

An example of a double displacement reaction occurs between sodium chloride and silver nitrate to form sodium nitrate and silver chloride.

Na-Cl(aq) + AgNO3(aq) –> NaNO3(aq) + Ag-Cl(s)


Acid-Base Reaction

An acid-base reaction is a type of double displacement reaction that occurs between an acid and a base. The H+ ion in the acid reacts with the OH- ion in the base to form water and an ionic salt:

The reaction between hydrobromic acid and sodium hydroxide is an example of an acid-base reaction:

H Br + Na-OH –> Na-Br + H2O

Oxidation-Reduction or Red-ox Reaction

In a red-ox reaction the oxidation numbers of atoms are changed. Red-ox reactions may involve the transfer of electrons between chemical species.

As an example, the reaction that occurs when iodide (I2) is reduced to Iodine (I-) and the thiosulfate (S2O32-) is oxidized:

2 S2O32−(aq) + I2(aq) –> S4O62−(aq) + 2 I−(aq)


Usually in a combustion reaction oxygen combines with another compound to form carbon dioxide and water. An example of a combustion reaction is the burning of naphthalene:

C10H8 + 12 O2 —> 10 CO2 + 4 H2O


In an isomerization reaction, the structural arrangement of a compound is changed but its net atomic composition remains the same.

Hydrolysis Reaction

A hydrolysis reaction involves water. The general form of a hydrolysis reaction is:

X-(aq) + H2O(l) <–> HX(aq) + OH-(aq)

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Bangladeshi Newspaper and Bangla Daily Newspaper

List of all Online Bang-la Newspapers:

The Newspaper of Bangladesh available.

Daily Prothom-alo

Daily amardesh




Daily Naya Diganta

Daily kaler kantho

Jai Jai Din

Bangladesh Pratidin

Daily Inqilab

Daily Manab Zamin

Daily Sangram

Daily Bhorer Kagoj




Shokaler Khabor

Daily Gonokantho

Bonik Barta

Amadar Orthoneeti

Bhorer Dak



Manob Kantha

Deener Shesha

Dainik Janata

Dainik Azadi

Al Ihsan

Bangladesh Shomoy

Desh Bangla

khabar patra

International News Agency

BBC Bangla

VOA News

Tehran Bangla Radio

German Bangla Radio

NHK World

Radio Russia

China Radio

Ananda Bazar




E kaler kantho

E Prothom-alo

E Samakal

E Janakontho

E Bonik Barta

Bangladesh Share Bazar News



Share Biz korcha

Share News 24

Stock Bangladesh

Regional Newspapers and News Agency

Daily Purbanchal


Suprobhat Bangladesh

Daily Shanama

Noakhali Web

Choloman Nokhali

Barisal News

khulna News



Amader Barisal

Probash News

Probasha Protidin

UK BD News


BNB News

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About the Eye function and Structure

Function &Eye Structure :

The human eye is the organ which gives us the sense of sight. It is elegant in its detail and design and houses many structures that work together to facilitate normal vision.


Eye Structure

Structures of the Eye

The orbit: The eyeball lies in a bony socket, known as the orbit. The orbit protects the eyeball. It is covered with fatty tissues which surround the eyeball and protect it from any external impact.

The Extra-ocular muscles: The eyes are attached to the wall of the orbit by six muscles, which help in the movement of the eyeball. These muscles are called extra-ocular muscles.

The Eyeball: The human eyeball is about 0.9 inches (24 mm) in diameter and is not perfectly round, being slightly flat in the front and back. It is not a sphere but an oblate spheroid.

The Conjunctiva: The conjunctiva is a thin, translucent membrane that covers the outer surface of the eye and the inner surface of the eyelids. The glands in the conjunctiva produce tear film that lubricates and protects the eye while it moves in its socket.

The Sclera: The sclera is the dense, white, fibrous outer protective coat of the eye, commonly known as “the white of the eye”.

The Cornea: The cornea is a transparent avascular watch glass like structure forming anterior 1/6th of the outer ?brous coat of the eyeball. Light waves entering the eye are maximally bent and focused by the cornea, which is then fine-tuned by the lens of the eye.

The Iris:  The iris is the coloured part of the eye and may be blue, green, gray, or brown. Depending on the amount of light in the external environment, iris can contract or relax to adjust the size of the pupil accordingly.

The ciliary body: The ciliary body is a tiny ring like structure present at the base of the iris. It changes the shape of the lens. It secretes aqueous humour, a fluid which provides nutrition to the eye.

The choroid: The choroid is a thin membrane lying beneath the scleroses. It absorbs light and prevents the light scattering.

The Lens:  The lens is a clear, transparent body which is biconvex, semi-solid, and shaped like an elongated sphere. It is located just behind the iris & pupil. Its principal purpose is to fine-tune the focusing done by the cornea.

The Retina: The retina is a thin film of tissue (like film in a camera) where images are brought into focus. Cells of retina receive light and transform it into image-forming signals which are transmitted through the optic nerve to the brain.

The Optic nerve: The optic nerve is the nerve that transmits visual information (image signals-nerve impulses) from the retina to the brain.

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Who are highly ambitious to prove his or her skill,you should test this puzzle and show your analytical ability.



Who are highly ambitious to prove his or her skill,you should test this puzzle and show your analytical ability.

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Wall paper Butterfly




Natural Beauty….

Nature view

Nature view

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About amino acid


There are two types of amino acids as per the nutritional requirement.They are classified into essential and non-essential amino acids.

Essential amino acids are those that are not synthesized by the body and are needed in the diet. Methionine, threonine, tryptophan, valine, isoleucine, leucine and phenylalanine are the essential amino acids.

Non-essential amino acids are those that are synthesized in the body and are not necessary in the diet. Glycine, alanine, serine, cysteine, tyrosine, proline, aspartic acid and glutamic acid are the non-essential amino acids.

Proteins are classified based on their composition. They are of two types:

Simple proteins
Simple proteins are those which contain only amino acids.Example: Egg albumin and seed globulin.
Conjugate proteins
Conjugate proteins are those which contain a non-amino acid component in addition to the amino acids. This non-amino acid component is called the prosthetic group. For e.g., glycoprotein (with carbohydrate as the prosthetic group), phosphoprotein (with phosphate as the prosthetic group), lipoprotein (with lipid as the prosthetic group).
Classification of Proteins According to Shape and Solubility:

Proteins can be broadly classified into three groups, based on their shape and solubility.
Membrane proteins:
These are protein which are in association with lipid membranes. Those membrane proteins that are embedded in the lipid bilayer have extensive hydrophobic amino acids that interact with the non-polar environment of the bilayer interior. Membrane proteins are not soluble in aqueous solution. Rhodopsin is an example of a membrane protein
Globular protein:
These are spherical and oval in shape, soluble in water and other solvents and digestable
a) albumin e.g. egg
b) globulin: soluble in neutral dilute salt solution e.g. serum globulin
c) proalamines: soluble in 70% alcohol e.g. gliadin and zein maize
d) histones: basic protein soluble in water and dilute acids

Fibrous proteins: These proteins have a rod like structure. They are not soluble in water. Collagen is an example of a fibrous protein.

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Who are highly ambitious to prove his or her skill,you should test this puzzle and show your analytical ability.puzzle 01

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 The International Pharmaceutical Federation (FIP) World Congress 2011 : Bangladesh at the Biggest Congress of Pharmacists and Pharmaceutical Scientists

  International Pharmaceutical Federation (FIP) is the global federation of national associations of pharmacists’ and pharmaceutical scientists around the world. Every year FIP hosts the most prestigious and one of a kind world congress for the pharmacists and the pharmaceutical scientists in different countries around the world. After several years of staying close to Europe, this year FIP organized it’s 71st International Congress of pharmacy and pharmaceutical sciences from, 3-8 September, 2011 in Hyderabad, India having the congress theme “Compromising Safety and Quality : A Risky Path”. The objective of the congress is to Network and connect with pharmacists and pharmaceutical scientists from all over the world.

The FIP Congress is the leading international event offering diverse learning opportunities for those active within all areas of pharmacy. The Congress is the ONLY true global event of its kind, where the pharmacists and the pharmaceutical scientists can become a part of a growing network. The 2011 FIP Congress in Hyderabad brought the participants to a new corner of the globe, but to a new level of connecting with others on a global platform of professional learning and growth. Around ‘2500’ pharmacists and scientists from around the world participated in the congress at Hyderabad International Convention Centre (HICC). FIP was honored to have the president of India ‘Srimati Prathibha Devisingh Patil’ who inaugurated the71st World Congress of Pharmacy and Pharmaceutical Sciences, 2011 and gave her speech for the  motivation of the  pharmacists’ potential around the world. Sentiments were also shared by other dignitaries attending the opening ceremonies including Dr. M Buchmann, The President of FIP; Dr. H Nakatani, Assistant Director General, World Health Organization (WHO); the Governorr, the Chief Minister, the Minister for Medical and Health Affair of Andhra Pradesh, India. The ground breaking parts of the opening ceremony was the official WHO-FIP Joint Statement signed on the Role of the Pharmacist in Tuberculosis Care and Control by FIP President Dr. Michel Buchmann and Assistant Director General of WHO Dr. H Nakatani, following the visit of the President and other Government Officials. The mentionable part is that considering the problem of Tuberculosis care in Bangladesh a group of pharmacists from Bangladesh received a  research grant from FIP to initiate and run a project on Tuberculosis. Bangladesh is one of the nine countries who was honored and privileged to receive this grant for the first time.

Going back to the main conference, it was charmed by several sessions with specific topic holding in each day. The chairs, speakers as well as the audiences in each session were the distinguished scientists, professors and health professionals including Tina Brock, Professor, University of California; Ian Bates, Professor, University of London; Timothy F Chen, Professor, University of Sydney; Takashi Kodama, President, Japan Pharmaceutical Association; Joseph Wang, President, FAPA; Morton P. Goldman, Asst Professor, Lerner college of Medicine, USA; Claire Anderson, Professor, University of Nottingham; Nahoko Kurosawa, Professor, Hokkaido Pharmaceutical University, Japan and many others from around the world.

From Bangladesh three delegates participated in the congress namely Mohammad Kawsar Sharif Siam currently studying in University College London(UCL), London,UK and graduated in Pharmacy from North South University (NSU), Dhaka, Bangladesh. Md. Khalilur Rahman and Muhammad Erfan Uddin, the students of Pharmacy in International Islamic University Chittagong (IIUC), Chittagong, Bangladesh.

It was a matter of honor for us as the new generation pharmacists of Banagladesh to learn and witness that Mohammad Kawsar Sharif Siam a pharmacist from Bangladesh was invited by FIP as a speaker to delivered a speech on “Counterfeit Medicine” on 6 September session infront of  around 200 distinguished scientists and health professionals. That session was hosted by Timothy F Chen, Professor, University of Sydney and Ema Paulino, CPS, Portugal.

In the another session, Bangladeshi delegate team represented the country attending the South East Asian FIP-WHO Forum of Pharmaceuticals ( SEARPharm ) Annual meeting, 2011. An organization consisting of eleven countries having five founding and six invited nations member.

Talking about the informal gathering in a formal congress, Taiwan hosted a reception party at the Congress Hall in HICC to show their own country’s cultural hospitality and Japan Pharmacy Assoication hosted a similar Japanese reception at Hotel Westin, India. Bangladesh, as an ever lasting friend nation of both Taiwan and Japan was invited to the receptions. Other than that sseveral general events like Council meeting, FIP Host Madsen Award Lecture, Assembly of Pharmacists, Poster sessions, Exhibitions, Welcome party, Hospital Pharmacy Section Welcome reception, YPG and IPSF International Evening took part during the whole week of the conference. On September 8 at the last day of congress, the closing event was arranged at Novotel Hotel with an enjoyable Gala Dinner.In 2012, FIP will celebrate it’s 100 year anniversary and as such will host the FIP centennial congress, taking place 3-8 October in Amsterdam, The Netherlands- the home country of FIP.

It was an eye opening experience for us, a congress where the health care professionals like scientists, professors are gathering under a roof sharing their views, cultures, activities and so on to one another. We believe by enhancing our participation in this sort of conferences can make up our information and research gap by exchanging ideas with modern world.

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2. List of Pharmaceutical companies in Bangladesh.

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The human Body



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amino acid

Simple Amino acid

Simple Amino acid

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Structure of protein

Protein Structure

Protein Structure

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On protein


Proteins are of both animal and plant origin. Some of the common sources are given bellow ..
# Groundnuts,
# beans,
# Whole cereals,
# Pulses.
# Among plants
# Fish Egg,
# Meat,
# Milk,
# Cheese among animal products.

Three dimensional structure of protein


The proteins are polymers made of monomers called the amino acids. There are 20 different kinds of amino acids that make up the proteins. However, they are present in different proportions in each of the proteins. The type and the sequence of amino acids in a protein are specified by the DNA in the cell that produces them. This sequence of amino acids is essential since it determines the overall structure and function of a protein.
Domains, motifs, and folds in protein structure proteins are made up of:
• Carbon (C)
• Hydrogen (H)
• Oxygen (O)
• Nitrogen (N)
• and some proteins contain Sulfur (S)
A protein is a natural polymer, made up of amino acid monomers joined together by peptide bonds (peptide or amide linkages).
• A dipeptide is made up of 2 amino acids joined together by a peptide bond (peptide or amide linkage)
• A tripeptide is made up of 3 amino acids joined together by peptide bonds (peptide or amide linkages)
• A tetrapeptide is made up of 4 amino acids joined together by peptide bonds (peptide or amide linkages)
• A polypeptide is made up of many amino acids joined together by peptide bonds (peptide or amide linkages)
A peptide bond (peptide or amide linkage) is a covalent bond formed between the carbon of the carboxyl group of one amino acid and the nitrogen of the amine group of another amino acid as shown below:
– C – N –

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