PURIFICATION AND CHARACTERIZATION OF CMP-NEUAC-GM1 (GA1-BETA-1-4GA1NAC) ALPHA-2-3 SIALYLTRANSFERASE FROM RAT-BRAIN

被引：16
|
作者：
GU, TJ [1 ]
GU, XB [1 ]
ARIGA, T [1 ]
YU, RK [1 ]
机构：
[1] VIRGINIA COMMONWEALTH UNIV,MED COLL VIRGINIA,DEPT BIOCHEM & MOLEC BIOPHYS,RICHMOND,VA 23298
来源：
FEBS LETTERS | 1990年 / 275卷 / 1-2期
关键词：
Ganglioside; Glycolipid; Glycosyltransferase; GM1; Sialyltransferase;
D O I：
10.1016/0014-5793(90)81444-S
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-NeuAc:GM1 α2-3sialyltransferase (GD1a synthase, 2.4.99.2) has been purified from the Triton extract of rat brain. The enzyme was purified and resolved by affinity chromatography on CDP-Sepharose column by a linear NaCl gradient elution. Final purification was achieved by elution from a 'GM1-acid'-Sepharose column. SDS-PAGE of the enzyme revealed a single protein band with an apparent Mr 44 kDa. It catalyzed specifically the sialylation of GD1b, GM1 and asialo-GM1. Enzyme products were identified by TLC in three different solvent systems, The Km value for GM1 was 7.5 × 10-2 M, and for CMP-NeuAc it was 6.5 × 10-5 M. © 1990.
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页码：83 / 86
页数：4
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