Biomaterial Database

Radioisotopic measurement of plasma kallikrein. 1982

G M Rodgers, and V H Donaldson, and M A Shuman

UI	MeSH Term	Description	Entries
D007610	Kallikreins	Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77).	Kallikrein,Kininogenase,Callicrein,Dilminal,Kallidinogenase,Kalliginogenase,Kallikrein A,Kallikrein B',Kallikrein Light Chain,Kinin-Forming Enzyme,Padutin,alpha-Kallikrein,beta-Kallikrein,beta-Kallikrein B,Enzyme, Kinin-Forming,Kinin Forming Enzyme,Light Chain, Kallikrein,alpha Kallikrein,beta Kallikrein,beta Kallikrein B
D007704	Kininogens	Endogenous peptides present in most body fluids. Certain enzymes convert them to active KININS which are involved in inflammation, blood clotting, complement reactions, etc. Kininogens belong to the cystatin superfamily. They are cysteine proteinase inhibitors. HIGH-MOLECULAR-WEIGHT KININOGEN; (HMWK); is split by plasma kallikrein to produce BRADYKININ. LOW-MOLECULAR-WEIGHT KININOGEN; (LMWK); is split by tissue kallikrein to produce KALLIDIN.	Cystatins, Kininogen,Kininogen,Prekinins,Prokinins,T-Kininogen,Thiostatin,Kininogen Cystatins,T Kininogen
D009842	Oligopeptides	Peptides composed of between two and twelve amino acids.	Oligopeptide
D002250	Carbon Radioisotopes	Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.	Radioisotopes, Carbon
D004789	Enzyme Activation	Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.	Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D005173	Factor XI Deficiency	A hereditary deficiency of blood coagulation factor XI (also known as plasma thromboplastin antecedent or PTA or antihemophilic factor C) resulting in a systemic blood-clotting defect called hemophilia C or Rosenthal's syndrome, that may resemble classical hemophilia.	Hemophilia C,Rosenthal Syndrome,Deficiency, Factor 11,Deficiency, Factor Eleven,Deficiency, Factor XI,Factor 11 Deficiency,Factor Eleven Deficiency,Plasma Thromboplastin Antecedent Deficiency,Rosenthal's Syndrome,Deficiencies, Factor 11,Deficiencies, Factor Eleven,Deficiencies, Factor XI,Factor 11 Deficiencies,Factor Eleven Deficiencies,Factor XI Deficiencies,Rosenthal Syndromes,Rosenthal's Syndromes,Rosenthals Syndrome,Syndrome, Rosenthal,Syndrome, Rosenthal's
D005174	Factor XII	Stable blood coagulation factor activated by contact with the subendothelial surface of an injured vessel. Along with prekallikrein, it serves as the contact factor that initiates the intrinsic pathway of blood coagulation. Kallikrein activates factor XII to XIIa. Deficiency of factor XII, also called the Hageman trait, leads to increased incidence of thromboembolic disease. Mutations in the gene for factor XII that appear to increase factor XII amidolytic activity are associated with HEREDITARY ANGIOEDEMA TYPE III.	Coagulation Factor XII,Hageman Factor,Factor 12,Factor Twelve
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006868	Hydrolysis	The process of cleaving a chemical compound by the addition of a molecule of water.
D014361	Trypsin Inhibitors	Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.	Trypsin Inhibitor,Inhibitor, Trypsin,Inhibitors, Trypsin