Reindarstellung und Analyse des Thrombininhibitors Hirudin
- 1 January 1967
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 348 (Jahresband), 1381-1386
- https://doi.org/10.1515/bchm2.1967.348.1.1381
Abstract
The thrombin inhibitor hirudin could be obtained from a prepurified preparation by chromato-graphy on DEAE-Sephadex with a specific activity of 10,400 antithrombin -units/mg. The inhibitor proved to be homogeneous by analysis in the ultracentrifuge and Tiselius-electrophoresis. Hirudin has the following amino acid composition: Asp10 Glu13 Cys Ser4 Gly9 Thr4 Ala1 Val3 Leu4 Ile2 Pro3 Phe2 Try2 His1 Lys4. Isoleucine was the N-terminal residue. The polypeptide inhibitor was destroyed by incubation with papain, pepsin and subtilopeptidase A and was resistant to plasmin, chymotrypsin A and trypsin.This publication has 7 references indexed in Scilit:
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