نتایج جستجو برای: tryptophanase

تعداد نتایج: 360  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1980
C Guidi-Rontani A Danchin A Ullmann

Pleiotropic carbohydrate-positive pseudorevertants have been isolated from a specific class of rho-crp double mutants of Escherichia coli carrying both defective transcription termination protein, rho, and cyclic AMP receptor protein. The modulation of catabolite repression of beta-galactosidase, amylomaltase, and tryptophanase has been studied in the pseudorevertants. It has been found that th...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1971
J Kuhn R L Somerville

A series of mutations has been isolated that confer upon amino-acid auxotrophs of Escherichia coli K-12 the ability to grow when fed various D-amino acids. Several distinct systems, mediating cellular use of the D-isomers of leucine, histidine, phenylalanine, tyrosine, tryptophan, isoleucine, and valine, can be mutationally activated. Mutations leading to D-tryptophan use (dadR) all map near pu...

Journal: :The Biochemical journal 1960
A N HALL J A LEESON H N RYDON J C TWEDDLE

The present paper is the second in a series designed to correlate substrate structure with the kinetic constants of enzyme-catalysed reactions and thus throw light on the nature of the attachment of the substrate to the enzyme. Since the preparation of the first paper (Nath & Rydon, 1954), which describes the influence of structure on the hydrolysis of substituted phenylf-D-glucosides by emulsi...

Journal: :The Journal of biological chemistry 1972
J B Li W E Knox

The loss of tryptophan oxygenase from rat livers after induction by hydrocortisone treatment was studied in living rats, isolated perfused livers, liver slices and cell-free preparations of these livers. Measurements of the enzyme by its activity and as an antigen were parallel except for apparently nonspecific inactivations in some incubations of cell-free preparations and the temporary, early...

Journal: :The Journal of biological chemistry 1972
N M Kredich B S Keenan L J Foote

The inducible enzyme, cysteine desulfhydrase, was purified from Salmonella fyphimurium to a state of near homogeneity. This enzyme has a very low tryptophanase activity, lacks cystathionase and tryptophan synthetase activities, and appears to be a specific cysteine desulfhydrase. The purified native enzyme has an s20,W of 10.4 and a molecular weight of 229,000 as determined by equilibrium sedim...

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