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Preparation and characterization of proteolyzed forms of human alpha-thrombin. 1988

P J Braun, and J Hofsteenge, and J Y Chang, and S R Stone
Friedrich Miescher Institut, Basel, Switzerland.

The kinetics of the tryptic digestion of human alpha-thrombin were studied. Based on the results of these studies a procedure for the preparation of highly purified, active human beta-thrombin was developed. This beta-thrombin contained less than 5% of other thrombin forms, was active towards tripeptidyl paranitroanilide substrates, but had lost more than 99% of its fibrinogen cleaving activity. Protein-chemical characterization of beta-thrombin showed that it had been cleaved at a single site (Arg73-Asn74) in the beta-chain, in contrast to human beta-thrombin obtained by autolysis, which is cleaved at both Arg-62 and Arg-73.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D013917 Thrombin An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN. Thrombase,Thrombin JMI,Thrombin-JMI,Thrombinar,Thrombostat,alpha-Thrombin,beta,gamma-Thrombin,beta-Thrombin,gamma-Thrombin,JMI, Thrombin
D014357 Trypsin A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. Tripcellim,Trypure,beta-Trypsin,beta Trypsin

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