Survey of neutral aminopeptidases in bovine, porcine, and chicken skeletal muscles.
A survey of the total aminopeptidase activity of bovine, porcine, and chicken skeletal muscles at neutral pH was done, using the beta-naphthylamide derivatives of nine amino acids, DEAE-cellulose column chromatography of the muscle extract found at least four types of aminopeptidases in porcine and chicken muscles. Aminopeptidase B and aminopeptidase C were commonly recognized in bovine, porcine, and chickens muscles. Hydrolase H was recognized in porcine and chicken muscles. Aminopeptidase nC and hydrolase H had high activity against almost all substrates. The substrate specificities of both enzymes were fairly compatible with the pattern of free amino acids which increased during the storage of bovine, porcine, and chicken meats [Agric. Biol. Chem. 52, 2323 (1988)], indicating that aminopeptidase C and hydrolase H are responsible for the increment of free amino acids during aging of these muscles.
Nishimura
T
T
Department of Agricultural Chemistry, The University of Tokyo, Japan
Okitani
A
A
Rhyu
M R
MR
Kato
H
H
D000577:Amides; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism*; D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology*; D013552:Swine
D000577:Amides; D000596:Amino Acids; D000626:Aminopeptidases