A new method is described for the preparation of pyruvate kinase from yeast. This eliminates proteolysis during the preparation. The molecular weight of yeast pyruvate kinase is 215000, and it is composed of four subunits. Such properties of the enzyme as its extinction coefficient, cold-lability, thiol-group reactivity and binding of Mn2+ ions are compared with those previously reported for yeast pyruvate kinase prepared by different methods. The specific activity is significantly higher than previously observed, but otherwise the enzyme is similar, apart from its molecular weight and Mn2+-binding characteristics, to preparations from Saccharomyces cerevisiae obtained in this laboratory (e.g. Fell et al., 1972, and references therein) and that of C. H. Suelter (e.g. Kuczenski & Suelter, 1971, and references therein), and is different from the enzyme isolated from Saccharomyces carlsbergensis by B. Hess and his co-workers (e.g. Wieker & Hess, 1972, and references therein).
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June 1974
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Research Article|
June 01 1974
The preparation and properties of pyruvate kinase from yeast
David A. Fell;
David A. Fell
1Nuffield Department of Clinical Biochemistry, Radcliffe Infirmary, University of Oxford, Oxford OX2 6HE, U.K.
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Peter F. Liddle;
Peter F. Liddle
1Nuffield Department of Clinical Biochemistry, Radcliffe Infirmary, University of Oxford, Oxford OX2 6HE, U.K.
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Arthur R. Peacocke;
Arthur R. Peacocke
1Nuffield Department of Clinical Biochemistry, Radcliffe Infirmary, University of Oxford, Oxford OX2 6HE, U.K.
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Raymond A. Dwek
Raymond A. Dwek
2Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1974 London: The Biochemical Society
1974
Biochem J (1974) 139 (3): 665–675.
Citation
David A. Fell, Peter F. Liddle, Arthur R. Peacocke, Raymond A. Dwek; The preparation and properties of pyruvate kinase from yeast. Biochem J 1 June 1974; 139 (3): 665–675. doi: https://doi.org/10.1042/bj1390665
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