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pro vyhledávání: '"Wayne B. Anderson"'
Publikováno v:
Analytical biochemistry. 221(1)
An intercompatible gene-tagging insert sequence was designed to conveniently introduce epitope-tagged polypeptides into bacteria and mammalian cells. The presence of rare restriction enzyme sites located between the ATG codon and the sequence encodin
Publikováno v:
Journal of Biological Chemistry. 246:5929-5937
A procedure is described for the purification of cyclic adenosine 3',5'-monophosphate receptor protein (CRP) from Escherichia coli involving chromatography on DEAE-cellulose and phosphocellulose, (NH4)2SO4 precipitation, and filtration on Sephadex G-
Publikováno v:
Proceedings of the National Academy of Sciences. 67:1417-1424
Regulation of glutamine synthetase (EC 6.3.1.2) in Escherichia coli is mediated by adenylylation and deadenylylation of the enzyme. The present studies show that one protein is a common component of both the adenylylation and deadenylylation systems.
Autor:
Robert L. Perlman, Ira Pastan, Max Gottesman, Peter Nissley, Benoit de Crombrugghe, Beatrice Chen, Wayne B. Anderson
Publikováno v:
Nature New Biology. 231:139-142
A cell free system has been developed in which only the components of the lactose operon are required for its transcription. Results obtained with this system suggest that the DNA of the operon contains a new regulator site, at which the cyclic AMP c
Autor:
Wayne B. Anderson, Ira Pastan
Publikováno v:
Biochimica et biophysica acta. 320(3)
An antiserum specific for the cyclic adenosine 3′,5′-monophosphate receptor from Escherichia coli has been employed to detect the presence of a similar protein in cellular extracts of a number of diverse organisms. In Ouchterlony double-diffusion
Autor:
Earl R. Stadtman, Wayne B. Anderson
Publikováno v:
Archives of biochemistry and biophysics. 143(2)
The deadenylylation of glutamine synthetase is catalyzed by the combined action of two, easily separable, protein components (P I and P II ). The P I component by itself catalyzes slow deadenylylation when it is adsorbed onto manganese phosphate prec
Treatment of unadenylylated glutamine synthetase from Escherichia coli with tetranitromethane or with N -acetylimidazole produces alterations in catalytic parameters that are similar to alterations caused by the physiologically important process of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6199c74965f4352b00033c92ea861d9f
https://europepmc.org/articles/PMC283082/
https://europepmc.org/articles/PMC283082/
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 67(4)
Two active forms of purified ATP:glutamine synthetase adenylyl-transferase from Escherichia coli are apparent on polyacrylamide gel electrophoresis at pH 8. The slower migrating component, which is identical to the P I -protein fraction of the glutam
Autor:
Wayne B. Anderson, Earl R. Stadtman
Publikováno v:
Biochemical and biophysical research communications. 41(3)
Previous studies showed that in Escherichia coli detachment of adenylyl groups from the adenylylated form of glutamine synthetase is catalyzed by a complex deadenylylation enzyme system composed of at least two protein components, and is activated by