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A search for electrophoretic variants of human adenine phosphoribosyl transferase

A search for electrophoretic variants of human adenine phosphoribosyl transferase Printed in Great Brituin A search for electrophoretic variants of human adenine phosphoribosyl transferase BY SUSAN MOWBRAY, B. WATSON AND HARRY HARRIS H . R .C. Human Biochemical Genetics Unit, The Galton Laboratorg, University College London Adenine phosphoribosyl transferase (APRT) catalyses the reaction of adenine with 5-pliosphoribosyl-pyrophosphate to give adenosine-5’-monophosphate and pyrophosphate. It is widely distributed in human tissues. There have been several reports of inherited variation of APRT in man. Kelley et nl. (1968) described a family in which four individuals showed a partial deficiency of the enzyme activity in red cells. The trait appeared to be inherited as an autosomal heterozygous character, and it did not appear to be associated with any obvious abnormality in uric acid production. Henderson et al. ( 1968) reported individual differences in therniostability of red cell APRT, which appeared to represent a common polymorphism involving two alleles, one produciiig a relatively more unstable form of the enzyme than the other. Bakay & Nyhan (1971) described the electrophoresis of APRT in acrylamide gels and reported that usually the enzyme migrated as a single symmetrical zone of activity, and in one individual a faster migrating variant was observed. I n the present paper http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annals of Human Genetics Wiley

A search for electrophoretic variants of human adenine phosphoribosyl transferase

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References (39)

Publisher
Wiley
Copyright
Copyright © 1972 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0003-4800
eISSN
1469-1809
DOI
10.1111/j.1469-1809.1972.tb00766.x
Publisher site
See Article on Publisher Site

Abstract

Printed in Great Brituin A search for electrophoretic variants of human adenine phosphoribosyl transferase BY SUSAN MOWBRAY, B. WATSON AND HARRY HARRIS H . R .C. Human Biochemical Genetics Unit, The Galton Laboratorg, University College London Adenine phosphoribosyl transferase (APRT) catalyses the reaction of adenine with 5-pliosphoribosyl-pyrophosphate to give adenosine-5’-monophosphate and pyrophosphate. It is widely distributed in human tissues. There have been several reports of inherited variation of APRT in man. Kelley et nl. (1968) described a family in which four individuals showed a partial deficiency of the enzyme activity in red cells. The trait appeared to be inherited as an autosomal heterozygous character, and it did not appear to be associated with any obvious abnormality in uric acid production. Henderson et al. ( 1968) reported individual differences in therniostability of red cell APRT, which appeared to represent a common polymorphism involving two alleles, one produciiig a relatively more unstable form of the enzyme than the other. Bakay & Nyhan (1971) described the electrophoresis of APRT in acrylamide gels and reported that usually the enzyme migrated as a single symmetrical zone of activity, and in one individual a faster migrating variant was observed. I n the present paper

Journal

Annals of Human GeneticsWiley

Published: Nov 1, 1972

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