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乳酸脱氢酶在固定化核苷酸上的亲和层析

Affinity chromatography of lactate dehydrogenase on immobilized nucleotides.

作者信息

Lowe C R, Dean P D

出版信息

Biochem J. 1973 Jul;133(3):515-20. doi: 10.1042/bj1330515.

DOI:10.1042/bj1330515
PMID:4354740
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1177729/
Abstract

The interaction of two isoenzymes of lactate dehydrogenase from pig heart muscle (H(4)) and rabbit skeletal muscle (M(4)), with immobilized nucleotides was examined: the effects of pH and temperature on the binding of lactate dehydrogenase were studied with immobilized NAD(+) matrices. The influence of substrate, product and sulphite on the binding of heart muscle lactate dehydrogenase to immobilized NAD(+) was investigated. The interaction of both lactate dehydrogenase isoenzymes with immobilized pyridine and adenine nucleotides and their derivatives were measured. The effects of these parameters on the interaction of lactate dehydrogenase with immobilized nucleotides were correlated with the known kinetic and molecular properties of the enzymes in free solution.

摘要

研究了猪心肌（H(4)）和兔骨骼肌（M(4)）乳酸脱氢酶的两种同工酶与固定化核苷酸的相互作用：用固定化NAD(+)基质研究了pH和温度对乳酸脱氢酶结合的影响。研究了底物、产物和亚硫酸盐对心肌乳酸脱氢酶与固定化NAD(+)结合的影响。测定了两种乳酸脱氢酶同工酶与固定化吡啶和腺嘌呤核苷酸及其衍生物的相互作用。这些参数对乳酸脱氢酶与固定化核苷酸相互作用的影响与游离溶液中酶已知的动力学和分子特性相关。

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引用本文的文献

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Biochem J. 1973 Jul;133(3):507-13. doi: 10.1042/bj1330507.

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