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A comparison of the kinetic properties of the common and rare variants of adenosine deaminase

A comparison of the kinetic properties of the common and rare variants of adenosine deaminase SUMMARY Adenosine deaminase activity has been measured in red cells from individuals of known ADA phenotype (ADA 1, ADA 2‐1, ADA 3‐1, ADA 3‐2) using adenosine and 2′‐deoxyadenosine as substrates. No significant differences were observed among the phenotypes in their relative deaminase activity with the two substrates. However, evidence suggests the occurrence of an uncommon allele designated ADA1wdetermining low levels of ADA activity. The deaminase activities of the phenotypes were in the order ADA 1 > ADA 2‐1 > ADA 3‐1 > ADA 3‐2 with both substrates. The relative activities of the alleles were estimated to be: ADA1 100%, ADA2 89%, ADA3 28% and ADA1 67% with adenosine, and ADA1 100%, ADA2 87%, ADA3 39% and ADA1 66% with 2′‐deoxyadenosine. The Michaelis constants for adenosine and 2'‐deoxyadenosine were determined for the different phenotypes. There were no significant differences in these values among the phenotypes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annals of Human Genetics Wiley

A comparison of the kinetic properties of the common and rare variants of adenosine deaminase

Annals of Human Genetics , Volume 45 (1) – Feb 1, 1981

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References (18)

Publisher
Wiley
Copyright
Copyright © 1981 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0003-4800
eISSN
1469-1809
DOI
10.1111/j.1469-1809.1981.tb00302.x
Publisher site
See Article on Publisher Site

Abstract

SUMMARY Adenosine deaminase activity has been measured in red cells from individuals of known ADA phenotype (ADA 1, ADA 2‐1, ADA 3‐1, ADA 3‐2) using adenosine and 2′‐deoxyadenosine as substrates. No significant differences were observed among the phenotypes in their relative deaminase activity with the two substrates. However, evidence suggests the occurrence of an uncommon allele designated ADA1wdetermining low levels of ADA activity. The deaminase activities of the phenotypes were in the order ADA 1 > ADA 2‐1 > ADA 3‐1 > ADA 3‐2 with both substrates. The relative activities of the alleles were estimated to be: ADA1 100%, ADA2 89%, ADA3 28% and ADA1 67% with adenosine, and ADA1 100%, ADA2 87%, ADA3 39% and ADA1 66% with 2′‐deoxyadenosine. The Michaelis constants for adenosine and 2'‐deoxyadenosine were determined for the different phenotypes. There were no significant differences in these values among the phenotypes.

Journal

Annals of Human GeneticsWiley

Published: Feb 1, 1981

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