Access the full text.
Sign up today, get DeepDyve free for 14 days.
Loading next page...
/lp/wiley/comparison-of-some-properties-of-red-cell-peptidase-a-from-weak-and-215HPYQn6r
References (12)
-
P. McAlpine, D. Hopkinson, H. Harris (1970)
Thermostability studies on the isozymes of human phosphoglucomutaseAnnals of Human Genetics, 34
-
(1964)
Mcditcrrancan variant of glucosc-6-phosphatc -
(1970)
Studies on the quantitative variation -
(1964)
34, 61. glucose-6-phosphate dehydrogenase in Gd A-and G d BMediterranean deficiency -
Kirkman Kirkman, Schettini Schettini, Pickabd Pickabd (1964)
Mediterranean, variant of glucoso‐G‐phosphate dehydrogenaseJ. Lab. Clin. Med., 63
-
MOAlfine MOAlfine, Hopkinson Hopkinson, Harris Harris (1970)
Thermostability studies on the isozymes of human phosphogfucomutaseAnn. Hum. Oenet. Lond., 34
-
A. Yoshida, A. Motulsky (1967)
Negro Variant of Glucose-6-Phosphate Dehydrogenase Deficiency (A-) in ManScience, 155
-
(1968)
I n vivo lability -
W. Lewis, H. Harris (1967)
Human Red Cell PeptidasesNature, 215
-
S. Piomelli, L. Corash, D. Davenport, J. Miraglia, E. Amorosi (1968)
In vivo lability of glucose-6-phosphate dehydrogenase in GdA- and GdMediterranean deficiency.The Journal of clinical investigation, 47 4
-
L. Luzzatto, N. Allan (1965)
Different properties of glucose 6-phosphate dehydrogenase from human erythrocytes with normal and abnormal enzyme levels.Biochemical and biophysical research communications, 21 6
-
K. Sinha, W. Lewis, G. Corney, H. Harris (1970)
Studies on the quantitative variation of human red cell peptidase A activityAnnals of Human Genetics, 34
- Publisher
- Wiley
- Copyright
- Copyright © 1971 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 0003-4800
- eISSN
- 1469-1809
- DOI
- 10.1111/j.1469-1809.1971.tb00244.x
- Publisher site
- See Article on Publisher Site
Abstract
SUMMARY Partially purified preparations of red‐cell peptidase A obtained from individuals with very weak and relatively strong activities have been compared, in order to see whether qualitative differences between the enzymes attributable to different alleles could be identified. It was found that the enzymes obtained both from the weak‐ and strong‐activity phenotypes were very similar in their pH‐activity curves, Michaelis constants, and elution profiles from DEAE‐cellulose and CM‐Sephadex columns. In comparisons of thermostability no marked differences were observed, but there was a suggestion that the enzyme in the weak‐activity phenotype may be slightly more thermostable than the enzyme in the strong‐activity phenotype.
Journal
Annals of Human Genetics – Wiley
Published: Feb 1, 1971