新型显色底物X-Y-对硝基苯胺存在下X-脯氨酰二肽基氨基肽酶的底物特异性研究。
Studies on substrate specificity of X-prolyl dipeptidyl-aminopeptidase during new chromogenic substrates, X-Y-p-nitroanilides.
作者信息
Kato T, Nagatsu T, Kimura T, Sakakibara S
出版信息
Experientia. 1978 Mar 15;34(3):319-20. doi: 10.1007/BF01923010.
PMID:631256
Abstract
Substrate specificity of X-prolyl dipeptidyl-aminopeptidase (dipeptidyl aminopeptidase IV) was examined by using newly synthesized 8 chromogenic substrates, X-Y-p-nitroanilides. Homogeneous enzyme from human submaxillary gland hydrolyzed glycylproline p-nitroanilide almost specifically, except alanylalanine p-nitroanilide which had 11% activity.
摘要
通过使用新合成的8种显色底物X-Y-对硝基苯胺，研究了X-脯氨酰二肽基氨基肽酶（二肽基氨基肽酶IV）的底物特异性。人下颌下腺的纯酶几乎特异性地水解甘氨酰脯氨酸对硝基苯胺，但丙氨酰丙氨酸对硝基苯胺有11%的活性。
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