Literature DB >> 6984543

Partial primary structure of human alpha 2-antiplasmin-homology with other plasma protease inhibitors.

H R Lijnen, B Wiman, D Collen.   

Abstract

Human alpha 2-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, alpha 1-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 alpha 2-antiplasmin also belongs to that superfamily. In addition, alpha 2-antiplasmin appeared to contain at least one internal homology.

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Year:  1982        PMID: 6984543

Source DB:  PubMed          Journal:  Thromb Haemost        ISSN: 0340-6245            Impact factor:   5.249


  1 in total

1.  The human alpha(2)-plasmin inhibitor: functional characterization of the unique plasmin(ogen)-binding region.

Authors:  Simon S Gerber; Sofia Lejon; Michael Locher; Johann Schaller
Journal:  Cell Mol Life Sci       Date:  2010-01-29       Impact factor: 9.261

  1 in total

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