| Literature DB >> 3394115 |
P J Braun1, J Hofsteenge, J Y Chang, S R Stone.
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.Entities:
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Year: 1988 PMID: 3394115 DOI: 10.1016/0049-3848(88)90228-9
Source DB: PubMed Journal: Thromb Res ISSN: 0049-3848 Impact factor: 3.944