[牛脑丙酮酸脱羧酶的纯化及某些性质]

[Purification and certain properties of pyruvate decarboxylase from bovine brain].

作者信息

Sabaliauskene V L, Glemzha A A

出版信息

Biokhimiia. 1976 Jul;41(6):1028-32.

Abstract

A procedure of isolation and purification of pyruvate decarboxylase (PDC) from bovine brain is worked out. 350-fold purified enzyme preparation was homogenous under polyacrylamide gel electrophoresis. Molecular weight of PDC from bovine brain was estimated to be 180 000 by means of gel chromatography through Sephadex G-200. The protein was eluted in two peaks (with molecular weight of 180 000 and 90 000 respectively). After the treatment of the enzyme preparation with 6 M guanidine chloride. Probably, partial dissociation of the enzyme molecule into two subunits takes place in this case. Data on paper chromatography confirmed that highly purified PDC preparations from bovine brain were isolated as apoenzyme, since they were almost free of TPP.

摘要

制定了从牛脑中分离和纯化丙酮酸脱羧酶（PDC）的方法。通过聚丙烯酰胺凝胶电泳，350倍纯化的酶制剂是均一的。通过Sephadex G-200凝胶色谱法估计牛脑PDC的分子量为180000。蛋白质以两个峰洗脱（分子量分别为180000和90000）。用6M氯化胍处理酶制剂后。在这种情况下，酶分子可能部分解离成两个亚基。纸色谱数据证实，从牛脑中分离出的高度纯化的PDC制剂是脱辅酶，因为它们几乎不含TPP。