title: Preparation and characterization of proteolyzed forms of human alpha-thrombin.
abstract: 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.
authors.affiliation: Friedrich Miescher Institut, Basel, Switzerland.
authors.forename: P J
authors.initials: PJ
authors.lastname: Braun
authors.forename: J
authors.initials: J
authors.lastname: Hofsteenge
authors.forename: J Y
authors.initials: JY
authors.lastname: Chang
authors.forename: S R
authors.initials: SR
authors.lastname: Stone
mesh_terms: D000596:Amino Acids / Q000032:analysis; D006801:Humans; D007700:Kinetics; D013917:Thrombin / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
chemical_list: D000596:Amino Acids; D014357:Trypsin; D013917:Thrombin