Thromb Haemost 1982; 48(03): 311-314
DOI: 10.1055/s-0038-1657288
Original Article
Schattauer GmbH Stuttgart

Partial Primary Structure of Human α2-Antiplasmin – Homology with Other Plasma Protease Inhibitors

H R Lijnen
The Center for Thrombosis and Vascular Research, Department of Medical Research, University of Leuven, Belgium
,
B Wiman
*   The Department of Clinical Chemistry, Umeå University Hospital, Umeå, Sweden
,
D Collen
The Center for Thrombosis and Vascular Research, Department of Medical Research, University of Leuven, Belgium
› Author Affiliations
Further Information

Publication History

Received 02 September 1982

Accepted 28 October 1982

Publication Date:
13 July 2018 (online)

Summary

Human α2-antiplasmin was digested with trypsin and with chymotrypsin and about 70 percent of the amino acids were sequenced and aligned in peptides ranging from 2 to 33 residues. Here we report five sequences of 21 to 33 residues. When these were compared with the primary structures of antithrombin III, α1-antitrypsin and ovalbumin, which belong to the same protein superfamily (Hunt and Dayhoff [1980] Biochem Biophys Res Commun 95: 864–871), three peptides showed clear homologies with these proteins, indicating that α2-antiplasmin also belongs to that superfamily. In addition, α2-antiplasmin appeared to contain at least one internal homology.

 
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