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一项关于人血清蛋白对α-烯醇化酶(EC 4.2.1.11)进行合成后修饰的研究。

A study on post-synthetic modifications in alfa-alfa enolase (EC 4.2.1.11) brought about by a human serum protein.

作者信息

Wevers R A, Boegheim J P, Hommes O R, van Landeghem A A, Mul-Steinbusch M W, van der Stappen J W, Soons J B

出版信息

Clin Chim Acta. 1984 May 30;139(2):127-35. doi: 10.1016/0009-8981(84)90321-8.

Abstract

Human alfa-alfa enolase is modified in the blood circulation by a serum protein for which the name 'modifying protein' is proposed. The protein occurs in every human serum tested and appears to be the same protein that is responsible for the post-synthetic modification in the M subunit of creatine kinase. Three alfa-alfa enolase forms, the original one plus two modified forms can be found in serum both in vivo and after in vitro incubation. The original alfa-alfa enolase is modified completely within a few hours in vitro in a pH-controlled human serum matrix at 37 degrees C. As the modification also takes place in vivo it is theoretically possible to acquire information about the activity of a disease process by doing one single determination of the amount of circulating alfa-alfa 3 enolase. A mechanism is proposed for the modification, where at first one of the two alfa chains is modified resulting in the alfa-alfa 2 form. Ultimately the second alfa chain is also modified. The alfa-alfa 1 form seems to be the completely modified alfa-alfa form. The three enolase forms differ in their isoelectric points but have similar Michaelis-Menten constants.

摘要

人α-α烯醇化酶在血液循环中被一种血清蛋白修饰,为此提出了“修饰蛋白”这一名称。在所检测的每个人类血清中均存在这种蛋白,且似乎与负责肌酸激酶M亚基合成后修饰的蛋白为同一蛋白。在体内及体外孵育后,血清中均可发现三种α-α烯醇化酶形式,即原始形式以及两种修饰形式。在37℃的pH值可控的人血清基质中,原始α-α烯醇化酶在体外几小时内即可被完全修饰。由于这种修饰也发生在体内,理论上通过单次测定循环中α-α3烯醇化酶的量就有可能获取有关疾病进程活性的信息。提出了一种修饰机制,首先两条α链中的一条被修饰,产生α-α2形式。最终第二条α链也被修饰。α-α1形式似乎是完全修饰后的α-α形式。这三种烯醇化酶形式的等电点不同,但米氏常数相似。

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