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New chromogenic substrates for X-prolyl dipeptidyl-aminopeptidase

✍ Scribed by Toshiharu Nagatsu; Masami Hino; Hiroshi Fuyamada; Taro Hayakawa; Shumpei Sakakibara; Yasuo Nakagawa; Tadashi Takemoto


Publisher
Elsevier Science
Year
1976
Tongue
English
Weight
670 KB
Volume
74
Category
Article
ISSN
0003-2697

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πŸ“œ SIMILAR VOLUMES


A new assay of X-prolyl dipeptidyl-amino
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A new assay procedure for X-prolyl dipeptidyl-aminopeptidase activity in human serum was developed with glycylproline p-phenylazoanilide tosylate as substrate. p-Phenylazoaniline liberated by the enzyme reaction was measured photometrically at 493 nm after stopping the reaction with acid. This assay

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The compound para-nitrobenzyloxycarbonylglycyl-(S-4-nitrobenzo-2-oxa- 1,3-diazole)-L-cysteinylglycine [NO2ZGly(S-NBD)CysGly] with an absorption maximum at 423 nm is readily hydrolyzed by angiotensin-converting enzyme (EC 3.4.15.1. peptidlyldipeptide hydrolase) to yield the S-benzfurazan derivative o