Further characterization of brain cholecystokinin-converting enzymes.
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.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D002766:Cholecystokinin / Q000032:analysis / Q000378:metabolism*; D002854:Chromatography, Paper; D004151:Dipeptides / Q000138:chemical synthesis / Q000378:metabolism; D004592:Electrophoresis, Starch Gel; D010450:Endopeptidases / Q000032:analysis / Q000378:metabolism*; D011863:Radioimmunoassay; D013379:Substrate Specificity
D004151:Dipeptides; D002766:Cholecystokinin; D010450:Endopeptidases; C019877:cholecystokinin converting enzyme