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Nuclotide Specificity of Pyruvatekinase Shizu Washio 1 1Department of Biochemistry, Faculty of Medicine, University of Tokyo pp.315-318
Published Date 1959/12/15
DOI https://doi.org/10.11477/mf.2425906105
  • Abstract
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 Nucleotide specificity of purified pyruvate kinases from muscle and baker's yeast was studied and the following results were obtained: (1) ADP, GDP, IDP, UDP, and CDP were effective as phosphate acceptor in both enzymes. Under the conditions tested the reaction velocities were in the ratio of ADP: GDP: UDP: IDP: CDP=100: 67: 18: 17: 10 in the muscle enzyme at pH 7.4, and ADP: UDP: CDP: IDP=100: 10: 6: 5: 3 in the yeast enzyme at pH 5.8.

 (2) Under the condition tested, the pH optima of the nucleotides were not so different from each other in the muscle enzyme, namely, they were 7.43, 7.37, 7.21, 7.38, and 7.50 in the cases of ADP, GDP, IDP, UDP, and CDP, respectively, whereas in the yeast enzyme they were rather different from each other, namely, 5.8, 5.8, 7.0, 6.0, and 7.0 in the cases of ADP, GDP, IDP, UDP, and CDP, respectively.


Copyright © 1959, THE ICHIRO KANEHARA FOUNDATION. All rights reserved.

基本情報

電子版ISSN 1883-5503 印刷版ISSN 0370-9531 金原一郎記念医学医療振興財団

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