Author:
Nakayama R,Kumagai H,Tochikura T
Abstract
Antiserum was prepared against the purified gamma-glutamyltranspeptidase (EC 2.3.2.2) of Proteus mirabilis. The antiserum inactivated the gamma-glutamyltranspeptidase activities of both purified enzyme and intact cells. Native cells were agglutinated with the antibody. Immunocytochemical studies with indirect immunofluorescence and electron microscopy analysis suggested that gamma-glutamyltranspeptidase is localized on the surface of the cell. Its distribution in the cell wall or periplasmic space or both was also confirmed by the treatment of cells with lysozyme-EDTA. The purified enzyme was activated by the addition of membrane phospholipids isolated from the same bacterium. The hydrolysis activity was stimulated more than the transpeptidation activity by several phospholipids.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference32 articles.
1. Phosphorus assay in column chromatography;Bartlett C. R.;J. Biol. Chem.,1959
2. A rapid method of total lipid extraction and purification;Bligh E. G.;Can. J. Biochem. Physiol.,1959
3. The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis;Boyland E.;Adv. Enzymol.,1969
4. Quantitative two-dimensional thinlayer chromatography of blood phospholipids;Broekhuyse R. M.;Clin. Chim. Acta,1969
5. Influence of phospholipids and their hydrolytic products on y-glutamyl transpeptidase activity;Butler J. D.;J. Biol. Chem.,1979
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