Affiliation:
1. Department of Biochemistry, The University of Texas Health Science Center, San Antonio, Texas 78284
Abstract
A particulate enzyme preparation from
Mycobacterium smegmatis
catalyzes the transfer of [
14
C]galactose from uridine 5′-diphosphate (UDP)-[
14
C]galactose and of [
14
C]glucose from UDP-[
14
C]glucose into chloroform-soluble products. The radioactive neutral lipids were purified by passage through diethylaminoethyl-cellulose, followed by thin-layer chromatography. When UDP-glucose was used as substrate, two major radioactive lipids were obtained; one had a hexose-glucose-glycerol ratio of 1:1:1. The second product had a hexose-glycerol ratio of 2:1 and, in addition to glucose, contained lesser amounts of mannose and galactose. With UDP-galactose as substrate, two radioactive products were observed that were chromatographically indistinguishable from the [
14
C]glucosyl-labeled mono- and diglycosyldiglyceride. Palmitate and oleate were the predominant fatty acid constituents in these lipids and were present in equimolar amounts in all of the products examined. The products have thus been identified as monoglycosyldiglyceride and a diglycosyldiglyceride containing glucose as the major hexose along with mannose and galactose. Properties of the galactosyl and glucosyl transferases are described.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
13 articles.
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