利用草氨酸-二氨基己基-琼脂糖亲和色谱法对D-和L-乳酸脱氢酶活性中心的研究
Studies on the active center of D- and L-lactate dehydrogenases using oxamate-diaminohexyl-Sepharose affinity chromatography.
作者信息
Tuengler P, Stein T N, Long G L
出版信息
Proc Natl Acad Sci U S A. 1980 Oct;77(10):5832-6. doi: 10.1073/pnas.77.10.5832.
Abstract
Vertebrate and invertebrate L-lactate dehydrogenases (L-lactate:NAD+ oxidoreductase, EC 1.1.1.27) are effectively bound to oxamate-diaminohexyl-Sepharose, whereas several D-lactate dehydrogenases (D-lactate:NAD+ oxidoreductase, EC 1.1.1.28) do not bind to the same Sepharose. One explanation for our findings is that the enzymes' substrate is oriented in a reversed manner in the active center of the D- and L-lactate dehydrogenases.
摘要
脊椎动物和无脊椎动物的L-乳酸脱氢酶（L-乳酸：NAD⁺氧化还原酶，EC 1.1.1.27）能有效地结合到草氨酸-二氨基己基-琼脂糖上，而几种D-乳酸脱氢酶（D-乳酸：NAD⁺氧化还原酶，EC 1.1.1.28）则不能结合到同样的琼脂糖上。对于我们的发现，一种解释是，在D-和L-乳酸脱氢酶的活性中心，酶的底物以相反的方式定向。
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