Partial purification of glycerophosphate acyltransferase from Escherichia coli
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چکیده
منابع مشابه
Purification and characterization of glycerophosphate acyltransferase from rat liver mitochondria.
Glycerophosphate acyltransferase (GAT) catalyzes the conversion of sn-glycerol 3-phosphate to lysophosphatidic acid (LPA), the first and committed step of triacylglycerol and phospholipid synthesis. In spite of the important regulatory roles GAT may play in this biosynthetic pathway, little information is available on the structure, biochemical properties, and regulation of GAT from eukaryotic ...
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CDP-diglyceride: L-serine phosphatidyltransferase (phosphatidylserine synthetase) of Escherichia coli is tightly associated with ribosomes in crude cell-free extracts. The synthetase has now been separated from ribosomes by extraction with solutions containing 5 M NaCl and has been purified loo-fold. The partially purified enzyme is devoid of contaminating hydrolytic activities and nearly free ...
متن کاملBiosynthesis of phosphatidyl glycerophosphate in Escherichia coli.
An enzyme (L-glycerol 3-phosphate: CMP phosphatidyltransferase) catalyzing the synthesis of phosphatidyl glycerophosphate from CDP-diglyceride and L-glycerol 3-phosphate has been rendered soluble by treatment of the particulate, membrane-containing fraction of E. coli with Triton X-100 and has been partially purified. The enzyme, devoid of phosphatidyl glycerophosphatase activity, is specific f...
متن کاملAcetylornithinase of Escherichia coli: partial purification and some properties.
Compounds Used-N”l-Acetyl-n-ornithine was synthesized as previously described (5, 3).’ L-Ornithine monohydrochloride was obtained from the Mann Research Laboratories. Several of the acetylamino acids used, including acetyl-nn-methionine, were supplied by the California Foundation for Biochemical Research.2 Organisms-The organisms used are E. coli (ATCC 9637) and ornithinerequiring mutant 160-37...
متن کاملMembrane phospholipid synthesis in Escherichia coli. Purification, reconstitution, and characterization of sn-glycerol-3-phosphate acyltransferase.
The membrane-bound sn-glycerol-3-phosphate acyltransferase of Escherichia coli was purified to near homogeneity from Triton X-100 extracts of membranes from strain vL3/pvL1 (Lightner, V. A., Larson, T. J., Tailleur, P., Kantor, G. D., Raetz, C. R. H., Bell, R. M., and Modrich, P. (1980) d Biol. Chem. 255, 9413-9420). This strain contains a hybrid plasmid bearing the pZsB gene, a structural gene...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1977
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.130.3.1072-1083.1977