Separation of carboxypeptidase A and B from longitudinal muscle layer of bovine small intestine: their properties regarding hydrolysis of enkephalins and enkephalin-analogs.
Carboxypeptidase A and B were partially purified from the soluble fraction of longitudinal muscle layer (myenteric plexus) of bovine small intestine. The obtained carboxypeptidase A hydrolyzed [Met]enkephalin-Arg6-Phe7 and [Leu]enkephalin, but [Met]enkephalin was not a suitable substrate for the enzyme. The Km value of carboxypeptidase A for [Met]enkephalin-Arg6-Phe7 was 0.74 mM and that for [Leu]enkephalin was 0.44 mM. Intestinal carboxypeptidase B hydrolyzed [Met]enkephalin-Arg6, liberating [Met]enkephalin, and the Km value of the enzyme for [Met]enkephalin-Arg6 was 0347 mM.
Kase
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R
Department of Medical Chemistry, Tokyo Metropolitan Institute of Medical Science, Japan.
Hideshima
C
C
Hazato
T
T
D000818:Animals; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000302:isolation & purification*; D043422:Carboxypeptidases A; D002417:Cattle; D004743:Enkephalin, Leucine / Q000378:metabolism*; D004744:Enkephalin, Methionine / Q000031:analogs & derivatives / Q000378:metabolism*; D007421:Intestine, Small / Q000201:enzymology*; D007700:Kinetics; D009197:Myenteric Plexus / Q000201:enzymology*
D004744:Enkephalin, Methionine; D004743:Enkephalin, Leucine; C027511:enkephalin-Met, Arg(6)-Phe(7)-; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D043424:Carboxypeptidase B