Facilitated Purification of Hypoxanthine Phosphoribosyltransferase

Facilitated Purification of Hypoxanthine Phosphoribosyltransferase Hop'pe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1379 -1 385, Oktober 1976 Wolf GUTENSOHN*, Marianne HUBER and Heidi JAHN Institut für Anthropologie und Humangenetik der Universität München (Received 9 June 1976) Summary: Three major approaches to the complete purification of hypoxanthine phosphoribosyltransferase from human erythrocytes and rat brain are described. Preparative isolelectric focusing which has been used for the isolation of the human enzyme was not fully successful in the case of rat brain. Preparative polyacrylamide-gel electrophoresis in gel blocks yields enzyme samples of high purity as judged by analytical gel electrophoresis, but with a comparatively low specific enzyme activity. The most rapid and convenient method, a modification of the affinity chromatography on GMP agarose first described by Hughes'5! gives hypoxanthine phosphoribosyltransferase which is superior to the other prepara- tions in its homogeneity and its specific activity. All three methods produce an identical enzyme protein detected by polyacrylamide electrophoresis on nondenaturing and sodium dodecylsulfate gels. Molecular data of hypoxanthine phosphoribosyltransferase derived from these studies are: Isoelectric points of 5.60; 5.85 and 5.90 for three isozyme peaks of the rat brain enzyme; and a molecular weight of 72000 for the native rat brain enzyme and of 25000 - 27000 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png hoppe-seyler's zeitschrift für physiologische chemie de Gruyter

Facilitated Purification of Hypoxanthine Phosphoribosyltransferase

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Publisher
de Gruyter
Copyright
Copyright © 1976 by the
ISSN
0018-4888
eISSN
1437-4315
DOI
10.1515/bchm2.1976.357.2.1379
Publisher site
See Article on Publisher Site

Abstract

Hop'pe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1379 -1 385, Oktober 1976 Wolf GUTENSOHN*, Marianne HUBER and Heidi JAHN Institut für Anthropologie und Humangenetik der Universität München (Received 9 June 1976) Summary: Three major approaches to the complete purification of hypoxanthine phosphoribosyltransferase from human erythrocytes and rat brain are described. Preparative isolelectric focusing which has been used for the isolation of the human enzyme was not fully successful in the case of rat brain. Preparative polyacrylamide-gel electrophoresis in gel blocks yields enzyme samples of high purity as judged by analytical gel electrophoresis, but with a comparatively low specific enzyme activity. The most rapid and convenient method, a modification of the affinity chromatography on GMP agarose first described by Hughes'5! gives hypoxanthine phosphoribosyltransferase which is superior to the other prepara- tions in its homogeneity and its specific activity. All three methods produce an identical enzyme protein detected by polyacrylamide electrophoresis on nondenaturing and sodium dodecylsulfate gels. Molecular data of hypoxanthine phosphoribosyltransferase derived from these studies are: Isoelectric points of 5.60; 5.85 and 5.90 for three isozyme peaks of the rat brain enzyme; and a molecular weight of 72000 for the native rat brain enzyme and of 25000 - 27000

Journal

hoppe-seyler's zeitschrift für physiologische chemiede Gruyter

Published: Jan 1, 1976

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