| trypsin | <enzyme> Serine protease from the pancreas of vertebrates. Cleaves peptide bonds involving the amino groups of lysine or arginine. (18 Nov 1997) |
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| trypsin G-banding stain | <technique> A unique chromosome staining technique, used in human cytogenetics to identify individual chromosomes, which produces characteristic bands. It utilises acetic acid fixation, air drying, denaturing chromosomes mildly with proteolytic enzymes, salts, heat, detergents, or urea, and finally Giemsa stain; chromosome bands appear similar to those fluorochromed by Q-banding stain. Synonym: Giemsa chromosome banding stain. (05 Mar 2000) |
| trypsin inhibitor | A peptide hydrolyzed off trypsinogen under the catalytic influence of enteropeptidase, with trypsin produced as a result; so called because the peptide masks or inhibits the active site of the trypsin molecule, one of the polypeptides, from various sources (e.g., human and bovine colostrum, soybeans, egg white), that inhibit the action of trypsin. Compare: Bowman-Birk inhibitor. (05 Mar 2000) |
| trypsin inhibitor, bowman-birk soybean | <chemical> A low-molecular-weight protein (minimum molecular weight 8000) which has the ability to inhibit trypsin as well as chymotrypsin at independent binding sites. It is characterised by a high cystine content and the absence of glycine. Pharmacological action: trypsin inhibitors. (12 Dec 1998) |
| trypsin inhibitor, kazal pancreatic | <chemical> A pancreatic trypsin inhibitor common to all mammals. It is secreted with the zymogens into the pancreatic juice. It is a protein composed of 56 amino acid residues and is different in amino acid composition and physiological activity from the kunitz bovine pancreatic trypsin inhibitor (aprotinin). Chemical name: Trypsin inhibitor, pancreatic secretory (12 Dec 1998) |
| trypsin inhibitor, kunitz soybean | <chemical> A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin. Pharmacological action: trypsin inhibitors. Chemical name: Trypsin inhibitor, Kunitz soybean (12 Dec 1998) |
| trypsin inhibitors | Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds. (12 Dec 1998) |
| trypsinogen | <physiology> The antecedent of trypsin, a substance which is contained in the cells of the pancreas and gives rise to the trypsin. Origin: Trypsin + -gen. Source: Websters Dictionary (01 Mar 1998) |
| a1-trypsin inhibitor | A glycoprotein that is the major protease inhibitor of human serum, is synthesised in the liver, and is genetically polymorphic due to the presence of over 20 alleles; individuals appropriately homozygous are deficient in a1-trypsin and are predisposed to pulmonary emphysema and juvenile hepatic cirrhosis because of alterations in the amino acid and sialic acid components of the glycoprotein. A1-Antitrypsin also inhibits thrombin. Synonym: a1-trypsin inhibitor, human a1-proteinase inhibitor. (05 Mar 2000) |
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| Artemia trypsin-like proteinase | <enzyme> Cysteine proteinase involved in lipovitellin degradation Registry number: EC 3.4.22.- (26 Jun 1999) |
| crystallised trypsin | A purified preparation of the pancreatic enzyme; used as an adjunct to surgery for debridement of necrotic wounds and ulcers. (05 Mar 2000) |
| soybean trypsin inhibitor | Single polypeptide (21 kD, 181 amino acids) that forms a stable, stoichiometric, enzymically inactive complex with trypsin. (18 Nov 1997) |