The kinetics and cytidine 5'-triphosphate (CTP) feedback inhibition of CTP synthetase in wild-type and four mutants of Chinese hamster V79 cells have been studied. The enzymes of the wild type and three of the four mutants exhibited positive cooperativity with the substrate uridine 5'-triphosphate (
Comparison of the properties of the alcohol dehydrogenases from wild-type and mutant Chinese hamster somatic cells
β Scribed by B. G. Talbot; J. P. Thirion
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 663 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-2928
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β¦ Synopsis
Alcohol dehydrogenases (alcohol: NAD oxidoreductase, E.C. 1.1.1.1.) from allyl alcohol-resistant and wild-type Chinese hamster cells were purified using gel filtration, ion-exchange, and affinity-column chromatography. Both enzymes exhibited the same isozyme band patterns on electrophoresis and isoelectric focusing. Physicochemical properties of the two enzymes such as pH and temperature optima, Km values, and temperature stability were found to be the same within the experimental errors. The genetic significance of these findings is discussed.
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