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[大鼠组织中肌酸激酶同工酶的测定]

[Determination of creatine kinase isoenzymes in rat tissues].

作者信息

Bukhanevich A M, Dmitrenko N P

出版信息

Ukr Biokhim Zh (1978). 1979 Jan-Feb;51(1):84-6.

PMID:425146
Abstract

A method is developed for detection and quantitative determination of the creatine kinase isoenzymes during electrophoresis in agar gel. They are found in the agar gel block by formation of fluorescent sites due to combination of the isoenzymes reaction product: creatine with ninhydride in the alkaline medium followed by fluorophore quantitative elution. The method is specific, simple, highly sensitive. It was used to study mobility of creatine kinase of mitochondria and isoenzymes of the rat myocardium mytochondria sarcoplasmic fraction during electrophoresis under different conditions. It is established that mobility of creatine kinase of mitochondria differs from that of isoenzymes. During electrophoresis in agar gel, contrary to polyacrylamide gel, it arranges relative to sarcoplasma isoenzymes depending on the buffer used.

摘要

本文开发了一种在琼脂凝胶电泳过程中检测和定量测定肌酸激酶同工酶的方法。由于同工酶反应产物:肌酸与碱性介质中的茚三酮结合形成荧光位点,然后对荧光团进行定量洗脱,从而在琼脂凝胶块中发现它们。该方法具有特异性、简单且高度灵敏。它被用于研究不同条件下电泳过程中大鼠心肌线粒体肌酸激酶和线粒体肌浆部分同工酶的迁移率。已确定线粒体肌酸激酶的迁移率与同工酶不同。在琼脂凝胶电泳过程中,与聚丙烯酰胺凝胶相反,它相对于肌浆同工酶的排列取决于所使用的缓冲液。

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