Determinants of tissue kallikrein cleavage specificity in the limited proteolysis of kininogens

Agents Actions Suppl. 1992:38 ( Pt 1):74-81. doi: 10.1007/978-3-0348-7321-5_10.

Abstract

Further evidence for interactions at tissue kallikrein extended binding sites, as determinants of the kininogen cleavage specificities is presented. Differences in the cleavage sites in kininogen hydrolysis by rat and other tissue kallikreins is related to subsite S1' specificity, while the low susceptibility of rat kininogen to horse tissue kallikrein is explained by the difference in their subsite S3'.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Horses
  • Humans
  • Hydrolysis
  • In Vitro Techniques
  • Kallikreins / metabolism*
  • Kinetics
  • Kininogens / metabolism*
  • Molecular Sequence Data
  • Oligopeptides / chemistry
  • Rats
  • Species Specificity
  • Substrate Specificity
  • Swine

Substances

  • Kininogens
  • Oligopeptides
  • Kallikreins