PURIFICATION TO HOMOGENEITY OF GD3 SYNTHASE AND PARTIAL-PURIFICATION OF GM3 SYNTHASE FROM RAT-BRAIN

被引：34

作者：

GU, XB ^{[1
]}

GU, TJ ^{[1
]}

YU, RK ^{[1
]}

机构：

[1] VIRGINIA COMMONWEALTH UNIV,MED COLL VIRGINIA,DEPT BIOCHEM & MOLEC BIOPHYS,RICHMOND,VA 23298

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 166卷 / 01期

关键词：

D O I：

10.1016/0006-291X(90)91957-T

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A CMP-sialic acid: GM3 sialyltransferase (GD3 synthase) and a CMP-sialic acid: LacCer sialyltransferas (GM3 synthase) have been purified 10,000- and 3,000-fold, respectively, from the Triton X-100 extract of rat brain. The two enzymes were purified and resolved by affinity chromatography on two successive CDP-Sepharose columns by NaCl gradient elution. Final purification of GD3 synthase was achieved by specific elution from a 'GM3 acid'-Sepharose column with buffer containing GM3. Sodium dodecylsulfate-gel electrophoresis of GD3 synthase revealed a single major protein band with an apparent molecular weight of 55,000. © 1990.

引用

页码：387 / 393

页数：7

共 14 条

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