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兔肝磷酸甘油酸脱氢酶的纯化及亚基结构

Purification and subunit structure of phosphoglycerate dehydrogenase from rabbit liver.

作者信息

Lund K, Merrill D K, Guynn R W

出版信息

Biochem J. 1986 Sep 15;238(3):919-22. doi: 10.1042/bj2380919.

Abstract

D-3-Phosphoglycerate dehydrogenase (EC 1.1.1.95) was purified from rabbit liver by (NH4)2SO4 fractionation, DEAE-Sephacel chromatography, affinity chromatography on AMP-agarose and molecular-sieve h.p.l.c. The purified enzyme was homogeneous as judged by SDS/polyacrylamide-slab-gel electrophoresis. On the basis of molecular-sieve h.p.l.c. and SDS/polyacrylamide-gel electrophoresis, the enzyme is a tetramer composed of subunits of Mr 60,000.

摘要

通过硫酸铵分级分离、DEAE-葡聚糖凝胶柱色谱法、AMP-琼脂糖亲和色谱法和高效液相分子筛色谱法从兔肝中纯化出D-3-磷酸甘油酸脱氢酶(EC 1.1.1.95)。通过十二烷基硫酸钠/聚丙烯酰胺平板凝胶电泳判断,纯化后的酶是均一的。基于高效液相分子筛色谱法和十二烷基硫酸钠/聚丙烯酰胺凝胶电泳,该酶是由分子量为60,000的亚基组成的四聚体。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18e/1147222/54adeb16d79e/biochemj00271-0289-a.jpg

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