Electrophoretic characterization of human phosphoribosylpyrophosphate synthetase

P. Boer; O. Sperling; A. De Vries

doi:10.1016/0006-2944(74)90020-9

Electrophoretic characterization of human phosphoribosylpyrophosphate synthetase

P. Boer^*, O. Sperling, A. De Vries

^*Corresponding author for this work

Clinical Biochemistry

Tel Aviv University

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Abstract

A method has been developed for the electrophoretic separation of 5-phosphoribosyl-1-pyrophosphate synthetase on cellulose acetate. The human enzyme in extracts of various tissues appears as a narrow symmetrical peak, indicating a single genotype. Similar results were obtained with rabbit and rat tissues. A mutant erythrocyte 5-phosphoribosyl-1-pyrophosphate synthetase from two siblings having gout associated with excessive purine production was found to have normal electrophoretic mobility.

Original language	English
Pages (from-to)	175-179
Number of pages	5
Journal	Biochemical Medicine
Volume	10
Issue number	2
DOIs	https://doi.org/10.1016/0006-2944(74)90020-9
State	Published - Jun 1974

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title = "Electrophoretic characterization of human phosphoribosylpyrophosphate synthetase",

abstract = "A method has been developed for the electrophoretic separation of 5-phosphoribosyl-1-pyrophosphate synthetase on cellulose acetate. The human enzyme in extracts of various tissues appears as a narrow symmetrical peak, indicating a single genotype. Similar results were obtained with rabbit and rat tissues. A mutant erythrocyte 5-phosphoribosyl-1-pyrophosphate synthetase from two siblings having gout associated with excessive purine production was found to have normal electrophoretic mobility.",

author = "P. Boer and O. Sperling and {De Vries}, A.",

year = "1974",

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AB - A method has been developed for the electrophoretic separation of 5-phosphoribosyl-1-pyrophosphate synthetase on cellulose acetate. The human enzyme in extracts of various tissues appears as a narrow symmetrical peak, indicating a single genotype. Similar results were obtained with rabbit and rat tissues. A mutant erythrocyte 5-phosphoribosyl-1-pyrophosphate synthetase from two siblings having gout associated with excessive purine production was found to have normal electrophoretic mobility.

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Electrophoretic characterization of human phosphoribosylpyrophosphate synthetase

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