Affiliation:
1. Department of Clinical Biochemistry, KB 3-01-1, Rigshospitalet, Copenhagen, Denmark.
2. Department of Chemistry, University of Copenhagen, DK-21 00 Copenhagen, Denmark.
Abstract
Mature alpha 2-plasmin inhibitor in human plasma has 12 more N-terminal residues than hitherto anticipated. The first residue is the methionine at position 28, downstream from the N-terminus of the pre-protein. The cDNA sequence predicts that the site cleaved upon formation of the mature inhibitor is a typical signal-peptidase recognition site. The mature inhibitor (464 residues) and the previously reported, and presumably degraded, form with N-terminal asparagine (452 residues), are present in plasma in about equal amounts. They both form a stable complex with plasmin. Recent studies on a recombinant alpha 2-plasmin inhibitor suggest that the 12 additional residues have functional implications [Sumi, Ichikawa, Nakamura, Miura and Aoki (1989) J. Biochem. 106, 703-707].
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
78 articles.
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