Phenotypic variation in the phosphotransferase activity of human red cell acid phosphatase (ACP1)
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics(clinical),Genetics
Link
http://link.springer.com/content/pdf/10.1007/BF00290961.pdf
Reference22 articles.
1. Bartlett GR (1959a) Human red cell glycolytic intermediates. J Biol Chem 234:449–458
2. Bartlett GR (1959b) Methods for the isolation of glycolytic intermediates by column chromatography with ion exchange resins. J Biol Chem 234:459–465
3. Burmaster CF (1946) Microdetermination of α-and β-glycerophosphates. J Biol Chem 164:233–240
4. Dissing J, Dahl O, Svensmark O (1979) Phosphonic and arsonic acids as inhibitors of human red cell acid phosphatase. Biochim Biophys Acta 569:159–176
5. Eze LC, Tweedie MCK, Bullen MF, Wren PSS, Evans DAP (1974) Quantitative genetics of human red cell acid phosphatase. Ann Hum Genet 37:333–340
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1. Human 18 kDa phosphotyrosine protein phosphatase (ACP1) polymorphism: studies of rare variants provide evidence that substitutions within or near alternatively spliced exons affect splicing result;Annals of Human Genetics;2000-03
2. Clinical and Biological Aspects of Acid Phosphatase;Critical Reviews in Clinical Laboratory Sciences;1995-01
3. Human Red Cell Acid Phosphatase (ACP1): Genetic Typing at the DNA Level;Advances in Forensic Haemogenetics;1994
4. The Molecular Basis of The “Red Cell” Acid Phosphatase Polymorphism;Advances in Forensic Haemogenetics;1994
5. Exon Structure at the Human ACP1 Locus Supports Alternative Splicing Model for f-Isozyme and s-Isozyme Generation;Biochemical and Biophysical Research Communications;1993-10
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