δ‐aminolevulinate dehydrase: a new genetic polymorphism in man
- 1 July 1981
- journal article
- Published by Wiley in Annals of Human Genetics
- Vol. 45 (3) , 223-229
- https://doi.org/10.1111/j.1469-1809.1981.tb00333.x
Abstract
A method has been developed for the electrophoretic and quantitative analyses of human red cell δ-aminolevulinate dehydrase (ALADH). The enzyme is under the control of an autosomal gene, with two common codominant alleles, ALADH1 and ALADH2, with frequencies of 0–89 and Oil, respectively, in the Italian population. Mean phenotypic enzyme activities are nearly identical: 52, 49 and 55 mlU/g Hb for ALADH 1, 2-1 and 2 phenotypes respectively.Keywords
This publication has 6 references indexed in Scilit:
- Purification and properties of uroporphyrinogen I synthase from human erythrocytes. Identification of stable enzyme-substrate intermediates.Published by Elsevier ,2021
- Purification and properties of delta-aminolevulinate dehydrase from human erythrocytes.Journal of Biological Chemistry, 1979
- Studies on the Inheritance of Human Erythrocyte σ-Aminolevulinate Dehydratase and Uroporphyrinogen SynthetaseEnzyme, 1973
- Linkage of Genes Controlling the Rate of Synthesis and Structure of Aminolevulinate DehydrataseScience, 1971
- Erythrocyte Delta‐Aminolaevulic Acid Dehydrase Activity in AnaemiaBritish Journal of Haematology, 1971
- Standardization of hemoglobinometry II. The hemiglobincyanide methodClinica Chimica Acta; International Journal of Clinical Chemistry, 1961