Zobrazeno 1 - 10
of 52
pro vyhledávání: '"R D DeMoss"'
Publikováno v:
Archives of Microbiology. 122:169-175
The conditions for synthesis, purification, and properties of tryptophanase by a marine organism (Vibrio K-7) were studied. Tryptophanase was induced by tryptophan and its analogs, and partially repressed by 0.5% glucose or glycerol. NaCl (0.4 M) was
Substrate-protein interaction in tryptophanase from Bacillus alvei. Kinetic and spectral evaluations
Autor:
J D Fenske, R D DeMoss
Publikováno v:
Journal of Biological Chemistry. 250:7554-7563
This investigation studied the substrate protein interaction of the alpha, beta elimination reaction in tryptophanase (EC 4.1.99.1). The results of this work are 2-fold. (a) The presence of multiple enzyme sites was found to be related to the observe
Autor:
K. Moser, R. D. DeMoss
Publikováno v:
Journal of Bacteriology. 98:167-171
The distribution of tryptophanase was studied. The highest observed specific activity, μmoles per minute per milligram (dry weight) cells, is given in parentheses after each species. Tryptophanase was inducible and repressible in Escherichia coli (.
Autor:
Sallie O'Neil Hoch, R. D. DeMoss
Publikováno v:
Journal of Biological Chemistry. 247:1750-1756
Ultracentrifugal analyses of native holotryptophanase of Bacillus alvei demonstrate that it has a molecular weight of 208,000 and a sedimentation coefficient of 9.7 S at infinite dilution. The tryptophanase molecule dissociates in the presence of 5 m
Autor:
Walter J. Dobrogosz, R. D. DeMoss
Publikováno v:
Biochimica et Biophysica Acta. 77:639-648
The general physiology of catabolite repression of l-arabinose isomerase (l-arabinose ketol-isomerase, EC 5.3.1.4) in Pediococcus pentosaceus has been investigated. Particular emphasis has been placed on the regulation of enzyme formation as influenc
Autor:
S. K. Griffiths, R. D. DeMoss
Publikováno v:
Journal of Bacteriology. 101:813-820
Tryptophanase from Bacillus alvei also possesses serine dehydratase activity. A comparison of this enzyme with l -serine dehydratase [ l -serine hydro-lyase (deaminating), EC 4.2.1.13] in toluene-treated whole cell preparations of the organism was un
Autor:
R. D. DeMoss, Martin Gibbs
Publikováno v:
Journal of Bacteriology. 70:730-734
Autor:
Leon Unger, R. D. DeMoss
Publikováno v:
Journal of Bacteriology. 91:1564-1569
Unger, Leon (University of Illinois, Urbana), and R. D. DeMoss . Metabolism of a proline analogue, l -thiazolidine-4-carboxylic acid, by Escherichia coli . J. Bacteriol. 91: 1564–1569. 1966.—Resting cells of Escherichia coli K-12, pregrown in a p
Autor:
Leonard Frank, R. D. DeMoss
Publikováno v:
Journal of Bacteriology. 77:776-782
Autor:
K. P. Gopinathan, R. D. DeMoss
Publikováno v:
Biochemistry. 7:1685-1691