Purification and properties of a collagenase inhibitor from cultures of bovine aorta

Joseph C. Nolan, Susan C. Ridge, Arnold L. Oronsky, S. S. Kerwar

Research output: Contribution to journalArticlepeer-review

Abstract

Bovine medial explants in culture synthesize a potent inhibitor of mammalian collagenase but not of bacterial collagenase. This inhibitor has been partially purified and has an apparent molecular weight of 45,000. It is a glycoprotein pro is stable to heat, trypsin, acid and mercurials. Inhibitory activity is destroyed on reductive alkylation. The inhibitor interacts with collagenase and this interaction leads to the loss of enzymatic activity. This inhibitor may play a physiological role in the control of collagen degradation in blood vessels.

Original languageEnglish (US)
Pages (from-to)93-102
Number of pages10
JournalAtherosclerosis
Volume35
Issue number1
DOIs
StatePublished - Jan 1980

Keywords

  • Atherosclerosis
  • Collagen turnover
  • Collagenase
  • Collagenase inhibitor

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine

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