| human a1-proteinase 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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| serine protease inhibitor | A class of highly polymorphic inhibitors of trypsin, elastase, and certain other proteases synthesised by hepatocytes and macrophages See: a1-antitrypsin. Synonym: serpins. (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) |
| noncompetitive inhibitor | <chemistry> Reversible inhibition of an enzyme by a compound that binds at a site other than the substrate binding site. (18 Nov 1997) |
| inhibitor | <chemistry, pharmacology> A molecule which represses or prevents another molecule from engaging in a reaction. See: inhibition. (09 Oct 1997) |
| inter-alpha-inhibitor | <chemical> Inhibits bovine trypsin and chymotrypsin; complex formed with chymotrypsin less stable; alpha-glycoprotein; shap - serum-derived hyaluronan associated protein Pharmacological action: serine proteinase inhibitors, trypsin inhibitors Chemical name: trypsin inhibitor, inter-alpha- Synonym: inter-alpha-trypsin inhibitor, protein pi, inter-alpha-trypsin inhibitor, heavy chain, shap protein (05 Dec 1998) |
| ovulation inhibitor | A compound that inhibits ovulation; often found in oral contraceptives. (05 Mar 2000) |
| tissue-inhibitor of metalloproteinase-1 | <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a n-glycosylated protein, molecular weight 28 kD, produced by a vast range of cell types and found in a variety of tissues and body fluids. It has been shown to suppress metastasis and inhibit tumour invasion in vitro. Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| tissue inhibitor-of metalloproteinase-2 | <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a 21 kD nonglycosylated protein found in tissue fluid and is secreted as a complex with progelatinase a by human fibroblast and uncomplexed from alveolar macrophages. An overexpression of timp-2 has been shown to inhibit invasive and metastatic activity of tumour cells and decrease tumour growth in vivo. Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| tissue inhibitor of-metalloproteinase-3 | <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a 21 kD, nonglycosylated protein. Timp-3 does not show a high degree of structural similarity unlike timp-1 and timp-2 which are structurally similar. However, it does possess a high degree of structural similarity with that of chicken timp-3 (chimp-3). Human timp-3 is of particular concern because of its potential role in cancer, arthritis, and eye diseases. Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| tissue inhibitor of metalloproteinases | <chemical> A family of secreted proteins (timp-1, timp-2, and timp-3) that play a crucial role in regulating the activity of the secreted metalloproteinases (collagenases, stromelysins, gelatinases). Of the three characterised, only timp-1 and timp-2 appear to have related primary structures and inhibitory properties. They influence the activation of the prometalloproteinase and act to modulate proteolysis of extracellular matrix, notably during tissue remodeling and inflammatory processes. On certain cell types, they can exhibit growth factor-like activity, and they can inhibit the tumourigenic and metastatic phenotype in cancer cells. (pharmacol ther 1993;59:329-41) Pharmacological action: antineoplastic agent, protease inhibitors. (12 Dec 1998) |
| 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) |