Author:
Holmes E,Boyer C,Preiss J
Abstract
Escherichia coli B glycogen synthase and branching enzyme, although similar in amino acid composition, had no significant immunological cross-reactivity. The N-terminal sequences of the glycogen synthase were rich in hydrophobic residues, whereas branching enzyme had a higher content of acidic and basic residues. However, residues 21 to 28 of glycogen synthase and 7 to 14 of branching enzyme shared six of eight residues in common. Two fractions of branching enzyme, branching enzymes I and II, which can be isolated from E. coli B cell extracts, have been shown to be immunologically identical, suggesting that only one type of branching enzyme activity is present in E. coli B. Evidence has been obtained which indicates that E. coli B glycogen synthase and branching enzyme are antigenically very similar to glycogen synthases and branching enzymes from other enteric bacteria. No cross-reactivity with either enzyme was observed in cell extracts from photosynthetic bacteria.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference35 articles.
1. Study of relationship among species of vibrio, photobacterium and terrestrial enterobacteria by an immunological comparison of glutamine synthetase and superoxide dismutase;Baumann L.;Curr. Microbiol.,1980
2. Studies of relationship among terrestrial Pseudomonas alcaligenes and enterobacteria by an immunological comparison of glutamine synthetase;Baumann L.;Arch. Microbiol.,1978
3. Biosynthesis of bacterial glycogen: purification and properties of Escherichia coli B a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase;Boyer C.;Biochemistry,1977
4. a-1,4-Glucan: a-1,4- glucan 6-glycosyltransferase from mammalian muscle;Brown B. I.;Methods Enzymol.,1966
5. The mechanism of the de novo synthesis of polysaccharide by phosphorylase;Brown D. H.;Proc. NatI. Acad. Sci. U.S.A.,1961
Cited by
26 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献