Further characterization of brain cholecystokinin-converting enzymes

Proc Natl Acad Sci U S A. 1980 Jun;77(6):3669-71. doi: 10.1073/pnas.77.6.3669.

Abstract

The brain cholecystokinin-converting enzymes that cleave intact cholecystokinin to its COOH-terminal dodecapeptide and octapeptide also cleave the synthetic dipeptides Arg-Ile (or Arg-Val or Arg-Leu) and Arg-Asp, respectively. Thus, they are not hormone-specific enzymes but are bond-specific. Ultracentrifuge studies demonstrate that there is Arg-Ile hydrolase activity associated with a protein greater in molecular weight than gamma globulin and that both Arg-Ile and Arg-Asp hydrolase activities are associated with one or more proteins between albumin and gamma globulin in molecular weight.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Brain / enzymology*
  • Cattle
  • Cholecystokinin / analysis
  • Cholecystokinin / metabolism*
  • Chromatography, Paper
  • Dipeptides / chemical synthesis
  • Dipeptides / metabolism
  • Electrophoresis, Starch Gel
  • Endopeptidases / analysis
  • Endopeptidases / metabolism*
  • Radioimmunoassay
  • Substrate Specificity

Substances

  • Dipeptides
  • Cholecystokinin
  • Endopeptidases
  • cholecystokinin converting enzyme