Structure and formation of microplasmin

Proc Natl Acad Sci U S A. 1987 Dec;84(24):8793-5. doi: 10.1073/pnas.84.24.8793.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Chromatography, High Pressure Liquid
  • Disulfides
  • Fibrinolysin* / biosynthesis
  • Humans
  • Hydrolysis
  • Peptide Fragments* / biosynthesis
  • Protein Conformation

Substances

  • Amino Acids
  • Disulfides
  • Peptide Fragments
  • microplasmin
  • Fibrinolysin