STUDIES OF A PHOSPHOLIPID-REQUIRING BACTERIAL ENZYME .I. PURIFICATION AND PROPERTIES OF URIDINE DIPHOSPHATE GALACTOSE - LIPOPOLYSACCHARIDE ALPHA-3-GALACTOSYL TRANSDERASE

被引：49
作者：
ENDO, A
ROTHFIELD, L
机构：
[1] Department of Molecular Biology, Albert Einstein College of Medicine, Bronx
[2] Department of Microbiology, University of Connecticut Health Center, Farmington, Conn.
来源：
BIOCHEMISTRY | 1969年 / 8卷 / 09期
关键词：
D O I：
10.1021/bi00837a003
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：
The uridine diphosphate galactose:lipopolysaccharide α-3-galactosyl transferase of Salmonella typhimurium requires phospholipid for activity and catalyzes one of the reactions involved in biosynthesis of the cell envelope lipopolysaccharide of the organism. The enzyme has now been purified approximately 6000-fold. The purified enzyme required phospholipid for activity and was inhibited in a competitive manner by closely related nonsubstrate lipopolysaccharides. Extraction of the purified enzyme with organic solvents removed a bound lipid-soluble component, which contained no phosphorus and is still unidentified. This component (lipid Y) caused aggregation of the enzyme, but no role of the lipid in the enzyme reaction itself has yet been established. © 1969, American Chemical Society. All rights reserved.
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页码：3500 / +
页数：1
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