Biomedical subjects
D A Hopkinson
Publications and source records attributed to D A Hopkinson.
A preliminary genetic interpretation of the esterase isozymes of human tissues.
1. The esterase isozymes of human tissues have been investigated using the technique of starch-gel electrophoresis. Conventional naphthyl-azo dye linked stains and new fluorogenic staining methods were used to detect the isozymes. 2. Multiple isozymes were identified in every tissue and they were characterized in terms of their electrophoretic mobility, tissue distribution, developmental changes in utero, substrate specificity, inhibition properties and molecular weight. On these criteria 13 sets of esterase isozymes were identified, in addition to the esterase isozymes due to cholinesterase and carbonic anhydrase. 3. The data suggest that the 13 sets of isozymes are determined by at least nine different structural gene loci. 4. No electrophoretic variants were identified in a limited population survey of post-mortem tissues from adults and foetuses, except for the previously described esterase D (ESD) phenotypes.
Aconitase polymorphism in man.
1. An electrophoretic method is described which resolves two groups of aconitase isozymes in human tissues, one group corresponding to the mitochondrial and the other to the soluble enzyme. This method has been used to screen human populations for electrophoretic variation. 2. Variant phenotypes of both the mitochondrial and the soluble aconitase are described, and family studies and sib-pair data demonstrate that the variation is genetically determined. 3. The variant isozyme patterns are accounted for in terms of allelic variation at two independent gene loci, ACONM and ACONS, which encode the mitochondrial and the soluble aconitase respectively. The electrophoretic survey has so far revealed two alleles at ACONM and seven alleles at ACONS. 4. The electrophoretic patterns shown by heterozygous individuals indicate that both soluble and mitochondrial aconitase are monomeric. The variant patterns also indicate that certain minor aconitase components resolved under the electrophoretic conditions employed represent 'secondary' isozymes of the primary translation products. 5. Population data on Europenas and Nigerians are presented and it is shown that both rare and common electrophoretic variants are segregating in the human species. The variation due to the three most common ACONS alleles in the Nigerians constitues a polymorphism.
Chromosome assignment of some human enzyme loci: mitochondrial malate dehydrogenase to 7, mannosephosphate isomerase and pyruvate kinase to 15 and probably, esterase D to 13.
Eleven independent man-mouse hybrids and 40 subclones from four to them were analysed for up to 42 enzyme markers. Nine subclones from three hybrid lines were fully karyotyped. The data presented suggest that the gene for the human enzyme MOR-M can be assigned to chromosome 7, whilst those for MPI and PK-3 are on chromosome 15. The use of a small number of well-characterized hybrids for gene assigments is discussed as well as the significance of some known human linkage relationships.
Assignment of the genes for human mitochondrial malate dehydrogenase to chromosome 7, for mannose phosphate isomerase and pyruvate kinase to chromosome 15, and, probably, for human esterase-D to chromosome 13 using man-mouse hybrids.
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Further data on the incidence and segregation of genetically determined electrophoretic variants of human red cell NADH diaphorase.
Human red cell NADH diaphorase isozyme patterns have been examined in 3,060 unrelated Australians of European origin, by starch gel electrophoresis. 26 people with variant isozyme patterns were encountered: 12 were phenotype Dia 2-1 and 13 were Dia 4-1. A new variant isozyme pattern (Dia 7-1) was identified. No variants were identified in 100 Melanesians and 70 Australian Aborigines.
Assignment of the genes for human mitochondrial malate dehydrogenase to chromosome 7, for mannose phosphate isomerase and pyruvate kinase to chromosome 15, and, probably, for human esterase-D to chromosome 13 using man-mouse hybrids.
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The incidence of rare alleles determining electrophoretic variants: data on 43 enzyme loci in man.
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Rare electrophoretic variants of glycerol-3-phosphate dehydrogenase: evidence for two structural gene loci (GPD1 and GPD2).
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The detection and differentiation of the products of the human carbonic anhydrase loci, CAI and CAII using fluorogenic substrates.
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A study of possible factors influencing the variation in liver alcohol dehydrogenase activity in individuals of the 'usual' ADH phenotype.
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Phosphoglucomutase (PGM2) variants in Trio Indians from Surinam.
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A trimeric structure for mammalian purine nucleoside phosphorylase.
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Genetic and non-genetic variation of triose phosphate isomerase isozymes in human tissues.
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Linkage data on Rh, PGM1, PGD, Peptidase C and Fy from family studies.
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Studies on the subunit structure and molecular size of the human alcohol dehydrogenase isozymes determined by the different loci, ADH1, ADH2, and ADH3.
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Studies on the properties of the human alcohol dehydrogenase isozymes determined by the different loci ADH1, ADH2, ADH3.
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