Inhibition of the endothelin-converting enzyme by pepsin digests of food proteins

Biosci Biotechnol Biochem. 1995 Feb;59(2):325-6. doi: 10.1271/bbb.59.325.

Abstract

Inhibitory activities toward the endothelin-converting enzyme (ECE) were detected in pepsin digests of bonito pyrolic appendix and beef. After Sep-Pak C18 fractionation, this activity from bonito and beef was recovered in the 50% and 25% ethanol fractions, respectively. Activities were also recovered in the ultrafiltrate (< 5000 Da), and disappeared after a pronase treatment. Therefore, these inhibitory activities may have peptidic properties.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aspartic Acid Endopeptidases / antagonists & inhibitors*
  • Cattle
  • Chemical Fractionation
  • Dietary Proteins / metabolism*
  • Endothelin-Converting Enzymes
  • Ethanol / chemistry
  • Food Handling
  • Meat
  • Metalloendopeptidases / antagonists & inhibitors*
  • Pepsin A / metabolism*
  • Pronase / metabolism
  • Tuna
  • Ultrafiltration

Substances

  • Dietary Proteins
  • Ethanol
  • Aspartic Acid Endopeptidases
  • Pepsin A
  • Metalloendopeptidases
  • Pronase
  • Endothelin-Converting Enzymes