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

H R Lijnen; B Wiman; D Collen

doi:10.1055/s-0038-1657288

Thrombosis and Haemostasis, Table of Contents

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

Abstract

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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.

Keywords

α₂-Antiplasmin - Primary structure - Homology

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References

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