Trypsin Inhibitors
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Trypsin Inhibitors
A trypsin inhibitor (TI) is a protein and a type of serine protease inhibitor (serpin) that reduces the biological activity of trypsin by controlling the activation and catalytic reactions of proteins. Trypsin is an enzyme involved in the breakdown of many different proteins, primarily as part of digestion in humans and other animals such as monogastrics and young ruminants. Serpins – including trypsin inhibitors – are irreversible and suicide substrate-like inhibitors. It destructively alters trypsin thereby rendering it unavailable to bind with proteins for the digestion process. NIHMSID 336639. As a result, protease inhibitors that interfere with digestion activity have an antinutritional effect. Therefore, trypsin inhibitors are considered an anti-nutritional factor or ANF. Additionally, trypsin inhibitor partially interferes with chymotrypsin function. Trypsinogen is an inactive form of trypsin, its inactive form ensures protein aspects of the body, such as the pancreas ...
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Serpin
Serpins are a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. The acronym serpin was originally coined because the first serpins to be identified act on chymotrypsin-like serine proteases (serine protease inhibitors). They are notable for their unusual mechanism of action, in which they irreversibly inhibit their target protease by undergoing a large conformational change to disrupt the target's active site. This contrasts with the more common competitive mechanism for protease inhibitors that bind to and block access to the protease active site. Protease inhibition by serpins controls an array of biological processes, including coagulation and inflammation, and consequently these proteins are the target of medical research. Their unique conformational change also makes them of interest to the structural biology and protein folding research communities. The conformational- ...
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NIH Manuscript Submission
PubMed Central (PMC) is a free digital repository that archives open access full-text scholarly articles that have been published in biomedical and life sciences journals. As one of the major research databases developed by the National Center for Biotechnology Information (NCBI), PubMed Central is more than a document repository. Submissions to PMC are indexed and formatted for enhanced metadata, medical ontology, and unique identifiers which enrich the XML structured data for each article. Content within PMC can be linked to other NCBI databases and accessed via Entrez search and retrieval systems, further enhancing the public's ability to discover, read and build upon its biomedical knowledge. PubMed Central is distinct from PubMed. PubMed Central is a free digital archive of full articles, accessible to anyone from anywhere via a web browser (with varying provisions for reuse). Conversely, although PubMed is a searchable database of biomedical citations and abstracts, the full ...
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Pancreas
The pancreas is an organ of the digestive system and endocrine system of vertebrates. In humans, it is located in the abdomen behind the stomach and functions as a gland. The pancreas is a mixed or heterocrine gland, i.e. it has both an endocrine and a digestive exocrine function. 99% of the pancreas is exocrine and 1% is endocrine. As an endocrine gland, it functions mostly to regulate blood sugar levels, secreting the hormones insulin, glucagon, somatostatin, and pancreatic polypeptide. As a part of the digestive system, it functions as an exocrine gland secreting pancreatic juice into the duodenum through the pancreatic duct. This juice contains bicarbonate, which neutralizes acid entering the duodenum from the stomach; and digestive enzymes, which break down carbohydrates, proteins, and fats in food entering the duodenum from the stomach. Inflammation of the pancreas is known as pancreatitis, with common causes including chronic alcohol use and gallstones. ...
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Bovine
Bovines (subfamily Bovinae) comprise a diverse group of 10 genera of medium to large-sized ungulates, including cattle, bison, African buffalo, water buffalos, and the four-horned and spiral-horned antelopes. The evolutionary relationship between the members of the group is still debated, and their classification into loose tribes rather than formal subgroups reflects this uncertainty. General characteristics include cloven hooves and usually at least one of the sexes of a species having true horns. The largest extant bovine is the gaur. In many countries, bovid milk and meat is used as food by humans. Cattle are kept as livestock almost everywhere except in parts of India and Nepal, where they are considered sacred by most Hindus. Bovids are used as draft animals and as riding animals. Small breeds of domestic bovid, such as the Miniature Zebu, are kept as pets. Bovid leather is durable and flexible and is used to produce a wide range of goods including clothing and bags. ...
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Lima Beans
A lima bean (''Phaseolus lunatus''), also commonly known as the butter bean, sieva bean, double bean, Madagascar bean, or wax bean is a legume grown for its edible seeds or beans. Origin and uses ''Phaseolus lunatus'' is found in Meso- and South America. Two gene pools of cultivated lima beans point to independent domestication events. The Mesoamerican lima bean is distributed in neotropical lowlands, while the other is found in the western Andes. They were discovered in Peru and may have been the first plant that was brought up under civilization by the native farmers. The Andes domestication took place around 2000 BC and produced a large-seeded variety (lima type), while the second, taking place in Mesoamerica around 800 AD, produced a small-seeded variety (Sieva type). By around 1300, cultivation had spread north of the Rio Grande, and, in the 1500s, the plant began to be cultivated in the Old World. The small-seeded (Sieva) type is found distributed from Mexico to Arg ...
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Alpha 1-antitrypsin
Alpha-1 antitrypsin or α1-antitrypsin (A1AT, α1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded in humans by the ''SERPINA1'' gene. A protease inhibitor, it is also known as alpha1–proteinase inhibitor (A1PI) or alpha1-antiproteinase (A1AP) because it inhibits various proteases (not just trypsin). In older biomedical literature it was sometimes called serum trypsin inhibitor (STI, dated terminology), because its capability as a trypsin inhibitor was a salient feature of its early study. As a type of enzyme inhibitor, it protects tissues from enzymes of inflammatory cells, especially neutrophil elastase, and has a reference range in blood of 0.9–2.3 g/L (in the US the reference range is expressed as mg/dL or micromoles), but the concentration can rise manyfold upon acute inflammation. When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessi ...
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Blood Plasma
Blood plasma is a light amber-colored liquid component of blood in which blood cells are absent, but contains proteins and other constituents of whole blood in suspension. It makes up about 55% of the body's total blood volume. It is the intravascular part of extracellular fluid (all body fluid outside cells). It is mostly water (up to 95% by volume), and contains important dissolved proteins (6–8%; e.g., serum albumins, globulins, and fibrinogen), glucose, clotting factors, electrolytes (, , , , , etc.), hormones, carbon dioxide (plasma being the main medium for excretory product transportation), and oxygen. It plays a vital role in an intravascular osmotic effect that keeps electrolyte concentration balanced and protects the body from infection and other blood-related disorders. Blood plasma is separated from the blood by spinning a vessel of fresh blood containing an anticoagulant in a centrifuge until the blood cells fall to the bottom of the tube. The blood plasm ...
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Molecular Weight
A molecule is a group of two or more atoms held together by attractive forces known as chemical bonds; depending on context, the term may or may not include ions which satisfy this criterion. In quantum physics, organic chemistry, and biochemistry, the distinction from ions is dropped and ''molecule'' is often used when referring to polyatomic ions. A molecule may be homonuclear, that is, it consists of atoms of one chemical element, e.g. two atoms in the oxygen molecule (O2); or it may be heteronuclear, a chemical compound composed of more than one element, e.g. water (two hydrogen atoms and one oxygen atom; H2O). In the kinetic theory of gases, the term ''molecule'' is often used for any gaseous particle regardless of its composition. This relaxes the requirement that a molecule contains two or more atoms, since the noble gases are individual atoms. Atoms and complexes connected by non-covalent interactions, such as hydrogen bonds or ionic bonds, are typically not consi ...
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ELISA
The enzyme-linked immunosorbent assay (ELISA) (, ) is a commonly used analytical biochemistry assay, first described by Eva Engvall and Peter Perlmann in 1971. The assay uses a solid-phase type of enzyme immunoassay (EIA) to detect the presence of a ligand (commonly a protein) in a liquid sample using antibodies directed against the protein to be measured. ELISA has been used as a diagnostic tool in medicine, plant pathology, and biotechnology, as well as a quality control check in various industries. In the most simple form of an ELISA, antigens from the sample to be tested are attached to a surface. Then, a matching antibody is applied over the surface so it can bind the antigen. This antibody is linked to an enzyme and then any unbound antibodies are removed. In the final step, a substance containing the enzyme's substrate is added. If there was binding, the subsequent reaction produces a detectable signal, most commonly a color change. Performing an ELISA involves at le ...
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Pressure Cooking
Pressure cooking is the process of cooking food under high pressure steam and water or a water-based cooking liquid, in a sealed vessel known as a ''pressure cooker''. High pressure limits boiling, and creates higher cooking temperatures which cook food far more quickly. The pressure cooker was invented in the seventeenth century by the physicist Denis Papin, and works by expelling air from the vessel, and trapping steam produced from the boiling liquid. This is used to raise the internal pressure up to one atmosphere above ambient and gives higher cooking temperatures between . Together with high thermal heat transfer from steam it permits cooking in between a half and a quarter the time of conventional boiling. Almost any food that can be cooked in steam or water-based liquids can be cooked in a pressure cooker. Modern pressure cookers have numerous safety features to prevent the pressure cooker from holding too much pressure. After cooking, the steam pressure is lowered b ...
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Chymotrypsinogen
Chymotrypsinogen is an inactive precursor (zymogen) of chymotrypsin, a digestive enzyme which breaks proteins down into smaller peptides. Chymotrypsinogen is a single polypeptide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. Release of the granules from the cell is stimulated by either a hormonal signal or a nerve impulse, and the granules spill into a duct leading into the duodenum. Activation Chymotrypsinogen must be inactive until it gets to the digestive tract. This prevents damage to the pancreas or any other organs. It is activated into its active form by another enzyme called trypsin. This active form is called π-chymotrypsin and is used to create α-chymotrypsin. Trypsin cleaves the peptide bond in chymotrypsinogen between arginine-15 and isoleucine-16. This creates two peptides within the π-chymotrypsin molecule, held together by a disulfide ...
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Trypsinogen
Trypsinogen () is the precursor form (or zymogen) of trypsin, a digestive enzyme. It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is cleaved to its active form, trypsin, by enteropeptidase, which is found in the intestinal mucosa. Once activated, the trypsin can cleave more trypsinogen into trypsin, a process called autoactivation. Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine. Function Trypsinogen is the proenzyme precursor of trypsin. Trypsinogen (the inactive form) is stored in the pancreas so that it may be released when required for protein digestion. The pancreas stores the inactive form trypsinogen because the active trypsin would cause severe damage to the tissue of the pancreas. Trypsinogen is released by the pancreas into the second part of the duodenum, via the pancreatic duct, along with other digestive enzymes. Activation of trypsinoge ...
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