The kinetic properties of yeast and muscle phosphoglyceric acid mutase.

V. Rodwell,J. C. Towne,S. Grisolía

Published 1957 in Journal of Biological Chemistry

ABSTRACT

During the past quarter of a century, the enzymes of the glycolytic scheme, with the exception of phosphoglyceric acid mutase, have been highly purified, and the properties of many of them have been investigated in detail. The first description of phosphoglyceric acid mutase by Meyerhof and Kiessling (1) arose from their discovery that phosphoglyceric acid isolated from yeast consisted of a mixture of 2and 3-phosphoglyceric acids. Sutherland, Posternak, and Cori (2,3) showed that 2,3-diphosphoglyceric acid, first isolated 25 years earlier by Greenwald (4), exhibited coenzyme activity for this enzyme. They also reported a partial purification of the enzyme from extracts of rabbit skeletal muscle and pointed out that these preparations contained diphosphoglycerate phosphatase activity. More recently, Cowgill and Pizer (5) have also reported a partial purification of mutasel from the same source and described some of its properties. The crystallization of mutase from bakers’ yeast has recently been reported by us (6). This paper presents a procedure for the preparation of a highly purified mutase from rabbit skeletal muscle. Although not crystalline, this preparation has a specific activity comparable to that of the crystalline yeast enzyme. In addition, we present a comparative study of the enzymatic

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