Affiliation:
1. Laboratory of Biochemistry, Section on Enzymes, National Heart Institute, National Institutes of Health, Bethesda, Maryland 20014
Abstract
The kinetic properties of
Escherichia coli
glutamine synthetase are markedly influenced by the manner in which the organism is grown. Enzyme obtained from stationary-phase cells grown on glycerol and glutamate is strongely inhibited by each of the eight feedback effectors known to influence this enzyme; however, the enzyme from log-phase cells grown on glucose and growth-limiting concentrations of NH
4
Cl is stimulated by some of these effectors. Of the growth variables examined, nitrogen source and time of harvest were the most important; carbon source and aeration seemed to have no effect. Two purified enzyme preparations have been obtained from cells grown under two different conditions, designated enzymes I and II for convenience. Enzyme I is stimulated by adenosine 5′-monophosphate, histidine, and tryptophan in the transfer assay, whereas enzyme II is strongly inhibited by all effectors tested. Enzyme I has a higher specific activity in the forward assay in the presence of Mg
++
or Co
++
, whereas enzyme II is more active in the presence of Mn
++
.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference9 articles.
1. Disc electrophoresis-IT. Method and application to human serum proteins;DAVIS B. J.;Ann. N. Y. Acad. Sci.,1964
2. Determination of serum proteins by means of the biuret reaction;GORNALL A. G.;J. Biol. Chem.,1949
3. Two E. coli glutamine synthetases with different sensitivities to feedback effectors;KINGDON H. S.;Biochem. Biophys. Res. Commun.,1967
4. The glutamyltransferase activity of normal and neoplastic tissues;LEVIN OW, L;J. Natl. Cancer Inst.,1954
5. MECKE D. K. WULFF AND H. HOLZER. 1966. 957
Cited by
81 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