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].
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Research Article| April 15 1993
Different N-terminal forms of α2-plasmin inhibitor in human plasma
A H Johnsen;
Biochem J (1993) 291 (2): 623–625.
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K Bangert, A H Johnsen, U Christensen, S Thorsen; Different N-terminal forms of α2-plasmin inhibitor in human plasma. Biochem J 15 April 1993; 291 (2): 623–625. doi: https://doi.org/10.1042/bj2910623
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