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一种用于测量半胱氨酰氨基肽酶活性的简单、精细的荧光测定方法。

Simple, refined fluorometric method for measuring cystyl-amino peptidase activity.

作者信息

Uete T, Morikawa M, Shimizu S, Shimano N, Konishi A

出版信息

Clin Biochem. 1977 Dec;10(6):193-6. doi: 10.1016/s0009-9120(77)92958-7.

Abstract

Cystyl-amino peptidase (EC 3.4.11.3) activity in serum or plasma was measured fluorometrically using L-cystine-di-beta-naphthylamide in the absence and presence of thiol such as mercaptoethanol. In the presence of thiol, L-cystine-di-beta-naphthylamide is converted to L-cysteine-beta-naphthylamide, and the enzyme activity to hydrolyze L-cysteine-beta-naphthylamide can be measured, while in the absence of thiol, the enzyme activity to hydrolyze L-cystine-di-beta-naphthylamide is determined. Thiol added did not affect various aminopeptidase activities. The present method is able to measure the enzyme activity hydrolyzing L-cystine-di-beta-naphthylamide and L-cysteine-beta-naphthylamide simultaneously and separately using only L-cysteine-di-beta-naphthylamide. This method is simple, sensitive and useful in clinical routine work, assessing placental function for the evaluation of the pregnant status.

摘要

使用L-胱氨酸-二-β-萘酰胺,在存在和不存在硫醇(如巯基乙醇)的情况下,通过荧光法测定血清或血浆中的胱氨酰氨基肽酶(EC 3.4.11.3)活性。在存在硫醇的情况下,L-胱氨酸-二-β-萘酰胺转化为L-半胱氨酸-β-萘酰胺,可以测量水解L-半胱氨酸-β-萘酰胺的酶活性,而在不存在硫醇的情况下,测定水解L-胱氨酸-二-β-萘酰胺的酶活性。添加的硫醇不影响各种氨基肽酶活性。本方法能够仅使用L-胱氨酸-二-β-萘酰胺同时且分别测量水解L-胱氨酸-二-β-萘酰胺和L-半胱氨酸-β-萘酰胺的酶活性。该方法简单、灵敏,在临床常规工作中对于评估胎盘功能以评价妊娠状态很有用。

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