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Proteolysis of Tropoelastin

  • Robert Mecham
  • Judith A. Foster
  • Carl Franzblau
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 79)

Abstract

The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS gels with molecular weights of approximately 57,000, 45,000, 36,000, 25,000 and 13–14,000.

Keywords

Caproic Acid Soybean Trypsin Inhibitor Chloromethyl Ketone Lower Molecular Weight Band Diethyldithiocarbamic Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Robert Mecham
    • 1
  • Judith A. Foster
    • 1
  • Carl Franzblau
    • 1
  1. 1.Department of BiochemistryBoston University School of MedicineBostonUSA

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