Cleavage specificities of individual members of kallikrein family of proteins on synthetic peptide containing the bradykinin sequence

J Protein Chem. 1998 Apr;17(3):291-4. doi: 10.1023/a:1022597004834.

Abstract

We have analyzed the effect on bond specificity of various isolated members of the mouse kallikrein family of proteins on a synthetic peptide containing the bradykinin sequence. The cleavage pattern shows the selected specificity of these proteases toward the synthetic peptide. The Phe-His bond (positions 11-12) in the synthetic peptide was favorably cleaved by most of the members in this family, including gamma nerve growth factor. On the other hand, the Lys-Arg bond (position 3-4) was found to be susceptible only to gamma-NGF. The combination of these cleavages could result in the degradation of bradykinin in vivo.

MeSH terms

  • Animals
  • Bradykinin / chemistry
  • Bradykinin / metabolism*
  • Kallikreins / isolation & purification
  • Kallikreins / metabolism*
  • Mice
  • Peptides / chemical synthesis
  • Peptides / metabolism*
  • Substrate Specificity

Substances

  • Peptides
  • Kallikreins
  • Bradykinin