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In vitro Synthesis of a Constitutive Enzyme of Escherichia coli, 6-phosphogluconate Dehydrogenase

โœ Scribed by Tomas Isturiz and Richard E. Wolf


Book ID
123653468
Publisher
National Academy of Sciences
Year
1975
Tongue
English
Weight
663 KB
Volume
72
Category
Article
ISSN
0027-8424

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๐Ÿ“œ SIMILAR VOLUMES


6-Phosphogluconate dehydrogenase in cell
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Investigations into the properties of 6-PG dehydrogenase in cell free extracts ofEscherichia coli revealed a pit optimum at pH 9.5 with a sharp decline on both sides of the optimum. The addition of 1.0 โ€ข 10 -3 ~ MgCI 2 produced maximal activity, whereas higher concentrations caused inhibition. The K

In vitro synthesis of enzymes of the try
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In vitro synthesis of enzymes of the tryptophan (trp) operon of E. coli was studied in an extract prepared from E. coli, which is programmed with purified DNA from trp transducing phages with mutations that effect the expression of the trp genes in various ways. Our results show that control of tran

In vitro synthesis of enzymes of the try
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A protein fraction, called At (= anti termination) factor, has been isolated from extracts of E. coli and partially purified. The At factor stimulates the synthesis in vitro of anthranilate synthetase, an enzyme encoded by two genes of the tryptophan (trp) operon, but has no effect on the synthesis