Pepsin Inhibitor
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Pepsin Inhibitor
Pepsin is an endopeptidase that breaks down proteins into smaller peptides. It is produced in the gastric chief cells of the stomach lining and is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site. It is one of three principal endopeptidases (enzymes cutting proteins in the middle) in the human digestive system, the other two being chymotrypsin and trypsin. There are also exopeptidases which remove individual amino acids at both ends of proteins (carboxypeptidases produced by the pancreas and aminopeptidases secreted by the small intestine). During the process of digestion, these enzymes, each of which is specialized in severing links between particular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the small ...
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Pepstatin
Pepstatin is a potent inhibitor of aspartyl proteases. It is a hexa-peptide containing the unusual amino acid statine (Sta, (3S,4S)-4-amino-3-hydroxy-6-methylheptanoic acid), having the sequence Isovaleryl-Val-Val-Sta-Ala-Sta (Iva-Val-Val-Sta-Ala-Sta). It was originally isolated from cultures of various species of Actinomyces due to its ability to inhibit pepsin at picomolar concentrations. Pepstatin A is well known to be an inhibitor of aspartic proteases such as pepsin, cathepsins D and E. Except for its role as a protease inhibitor, however, the pharmacological action of pepstatin A upon cells remain unclear. Pepstatin A suppresses receptor activator of NF-κB ligand (RANKL)–induced osteoclast differentiation. Pepstatin A suppresses the formation of multinuclear osteoclasts dose-dependently. This inhibition of the formation only affected osteoclast cells, i.e., not osteoblast-like cells. Furthermore, pepstatin A also suppresses differentiation from pre-osteoclast cells to mo ...
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Small Intestine
The small intestine or small bowel is an organ in the gastrointestinal tract where most of the absorption of nutrients from food takes place. It lies between the stomach and large intestine, and receives bile and pancreatic juice through the pancreatic duct to aid in digestion. The small intestine is about long and folds many times to fit in the abdomen. Although it is longer than the large intestine, it is called the small intestine because it is narrower in diameter. The small intestine has three distinct regions – the duodenum, jejunum, and ileum. The duodenum, the shortest, is where preparation for absorption through small finger-like protrusions called villi begins. The jejunum is specialized for the absorption through its lining by enterocytes: small nutrient particles which have been previously digested by enzymes in the duodenum. The main function of the ileum is to absorb vitamin B12, bile salts, and whatever products of digestion that were not absorbed by the ...
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John Howard Northrop
John Howard Northrop (July 5, 1891 – May 27, 1987) was an American biochemist who, with James Batcheller Sumner and Wendell Meredith Stanley, won the 1946 Nobel Prize in Chemistry. The award was given for these scientists' isolation, crystallization, and study of enzymes, proteins, and viruses. Northrop was a Professor of Bacteriology and Medical Physics, Emeritus, at University of California, Berkeley. Biography Early years Northrop was born in Yonkers, New York to John Isaiah, a zoologist and instructor at Columbia University who is a member of the Havemeyer family, and Alice Rich Northrop, a teacher of botany at Hunter College. His father died in a lab explosion two weeks before John H. Northrop was born. The son was educated at Yonkers High School and Columbia University, where he earned his BA in 1912 and PhD in chemistry in 1915. During World War I, he conducted research for the U.S. Chemical Warfare Service on the production of acetone and ethanol through ferme ...
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Protein Crystallization
Protein crystallization is the process of formation of a regular array of individual protein molecules stabilized by crystal contacts. If the crystal is sufficiently ordered, it will diffract. Some proteins naturally form crystalline arrays, like aquaporin in the lens of the eye. In the process of protein crystallization, proteins are dissolved in an aqueous environment and sample solution until they reach the supersaturated state. Different methods are used to reach that state such as vapor diffusion, microbatch, microdialysis, and free-interface diffusion. Developing protein crystals is a difficult process influenced by many factors, including pH, temperature, ionic strength in the crystallization solution, and even gravity. Once formed, these crystals can be used in structural biology to study the molecular structure of the protein, particularly for various industrial or medical purposes. Development of protein crystallization For over 150 years, scientists from all aroun ...
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Ancient Greek
Ancient Greek includes the forms of the Greek language used in ancient Greece and the ancient world from around 1500 BC to 300 BC. It is often roughly divided into the following periods: Mycenaean Greek (), Dark Ages (), the Archaic period (), and the Classical period (). Ancient Greek was the language of Homer and of fifth-century Athenian historians, playwrights, and philosophers. It has contributed many words to English vocabulary and has been a standard subject of study in educational institutions of the Western world since the Renaissance. This article primarily contains information about the Epic and Classical periods of the language. From the Hellenistic period (), Ancient Greek was followed by Koine Greek, which is regarded as a separate historical stage, although its earliest form closely resembles Attic Greek and its latest form approaches Medieval Greek. There were several regional dialects of Ancient Greek, of which Attic Greek developed into Koine. Dia ...
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Theodor Schwann
Theodor Schwann (; 7 December 181011 January 1882) was a German physician and physiologist. His most significant contribution to biology is considered to be the extension of cell theory to animals. Other contributions include the discovery of Schwann cells in the peripheral nervous system, the discovery and study of pepsin, the discovery of the organic nature of yeast, and the invention of the term "metabolism". Early life and education Theodor Schwann was born in Neuss on 7 December 1810 to Leonard Schwann and Elisabeth Rottels. Leonard Schwann was a goldsmith and later a printer. Theodor Schwann studied at the Dreikönigsgymnasium (also known as the Tricoronatum or Three Kings School), a Jesuit school in Cologne. Schwann was a devout Roman Catholic. In Cologne his religious instructor , a priest and novelist, emphasized the individuality of the human soul and the importance of free will. In 1829, Schwann enrolled at the University of Bonn in the premedical curriculum. ...
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Swiss Institute Of Bioinformatics
The SIB Swiss Institute of Bioinformatics is an academic not-for-profit foundation which federates bioinformatics activities throughout Switzerland. The institute was established on 30 March 1998 and its mission is to provide core bioinformatics resources to the national and international life science research community in fields such as genomics, proteomics and systems biology as well as to lead and coordinate the field of bioinformatics in Switzerland. In particular, it promotes research, develops databanks and computer technologies, and is involved in teaching and service activities. History The institute was originally created to provide a framework for stable long-term funding for both the Swiss-Prot database and the Swiss EMBnet node. Swiss-Prot in particular went through a major funding crisis in 1996, which led the leaders of the five research groups active in bioinformatics in Geneva and Lausanne, Ron Appel, Amos Bairoch, Philipp Bucher, Victor Jongeneel a ...
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Gastric Acid
Gastric acid, gastric juice, or stomach acid is a digestive fluid formed within the stomach lining. With a pH between 1 and 3, gastric acid plays a key role in digestion of proteins by activating digestive enzymes, which together break down the long chains of amino acids of proteins. Gastric acid is regulated in feedback systems to increase production when needed, such as after a meal. Other cells in the stomach produce bicarbonate, a base, to buffer the fluid, ensuring a regulated pH. These cells also produce mucus – a viscous barrier to prevent gastric acid from damaging the stomach. The pancreas further produces large amounts of bicarbonate and secretes bicarbonate through the pancreatic duct to the duodenum to neutralize gastric acid passing into the digestive tract. The active components of gastric acid are protons and chloride. Often simplistically described as hydrochloric acid, these species are produced by parietal cells in the gastric glands in the stomach. The sec ...
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Hydrochloric Acid
Hydrochloric acid, also known as muriatic acid, is an aqueous solution of hydrogen chloride. It is a colorless solution with a distinctive pungent smell. It is classified as a strong acid Acid strength is the tendency of an acid, symbolised by the chemical formula HA, to dissociate into a proton, H+, and an anion, A-. The dissociation of a strong acid in solution is effectively complete, except in its most concentrated solutions .... It is a component of the gastric acid in the digestive systems of most animal species, including humans. Hydrochloric acid is an important laboratory reagent and industrial chemical. History In the early tenth century, the Persian physician and alchemist Abu Bakr al-Razi ( 865–925, Latin: Rhazes) conducted experiments with sal ammoniac (ammonium chloride) and vitriol (hydrated sulfates of various metals), which he distilled together, thus producing the gas hydrogen chloride. In doing so, al-Razi may have stumbled upon a primitive method ...
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Zymogen
In biochemistry, a zymogen (), also called a proenzyme (), is an inactive precursor of an enzyme. A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme. The biochemical change usually occurs in Golgi bodies, where a specific part of the precursor enzyme is cleaved in order to activate it. The inactivating piece which is cleaved off can be a peptide unit, or can be independently-folding domains comprising more than 100 residues. Although they limit the enzyme's ability, these N-terminal extensions of the enzyme or a “prosegment” often aid in the stabilization and folding of the enzyme they inhibit. The pancreas secretes zymogens partly to prevent the enzymes from digesting proteins in the cells in which they are synthesised. Enzymes like pepsin are created in the form of pepsinogen, an inactive zymogen. Pepsinogen is activated when chief ce ...
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