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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1987 Dec;84(24):8793–8795. doi: 10.1073/pnas.84.24.8793

Structure and formation of microplasmin.

H L Wu 1, G Y Shi 1, R C Wohl 1, M L Bender 1
PMCID: PMC299636  PMID: 2962191

Abstract

The structure of human microplasmin, prepared from plasmin in alkaline solution, has been studied. Microplasmin consists of two polypeptide chains connected by disulfide bonds. One polypeptide is the B chain of plasmin consisting of 230 amino acids, and the other peptide is the COOH-terminal portion of the A chain of plasmin consisting of 31 amino acid residues. Microplasmin has a molecular weight of 28,635, calculated from its primary sequence. It is slightly more positively charged than plasminogen and is a more hydrophobic molecule. The proposed scheme for the formation of microplasmin involves autolysis at specific peptide bonds and scrambling of especially sensitive disulfide bonds in alkaline solution.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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