Biochemical genetic analysis of human and rodent aldehyde dehydrogenase (ALDH)

Hopkinson, D. A.; Santistéban, Inés; Povey, Sue; Smith, Moyra

doi:10.1016/0741-8329(85)90019-9

Cited by 14 publications

(2 citation statements)

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“…Occasional samples, about 1 in 25 in the European population, show a variant 3-banded isozyme pattern (track 2, Fig. 1) which is believed to represent heterozygosity at the ALDH3 locus, since the variation was reproducible in lung and stomach specimens from the same individuals (Hopkinson et al 1985). Attempts to carry out family studies of this polymorphism using easily accessible tissues such as erythrocytes and leukocytes from the blood, cultured fibroblasts and lymphoblastoid cells, were frustrated by the total absence of ALDH3 from this material.…”

Section: Methodsmentioning

confidence: 99%

“…The discovery of genetically determined deficiency of ALDHB in Oriental populations (Goedde, Harada & Agarwal, 1979) and the identification of electrophoretic variants of ALDHS in Indian (Teng, 1981) and European (Hopkinson et al 1985) individuals suggest that these two sets of isozymes are coded by separate structural genes. Furthermore, since these genetic polymorphisms are independent and are not associated with quantitative or qualitative variation of ALDHl or ALDH4, it seems likely that all four sets of ALDH isozymes are coded independently.…”

Section: Introductionmentioning

confidence: 99%

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Chromosome assignment, biochemical and immunological studies on a human aldehyde dehydrogenase, ALDH3

Santistéban

Povey

West

et al. 1985

Annals of Human Genetics

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The biochemical properties of ALDH isozymes have been examined in human tissues and one set, designated ALDH3, has been studied in detail. These components occur at highest levels in lung and stomach, but were not expressed in fetal tissues, or in blood, hair roots and fibroblasts. The ALDH3 isozymes show optimal activity with benzaldehyde and can use either NAD or NADP as cofactor. Antiserum against a partially purified ALDH3, from stomach, selectively precipitates this isozyme from human tissues and selectively recognizes an homologous component in the rat. Human and rodent ALDH3 were not immunoprecipitated by anti-ALDH1 or anti-ALDH2 antisera. High levels of expression were found in human-rodent hybrids, constructed using rat hepatoma cells, and these hybrids were used to assign the human ALDH3 gene to chromosome 17.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%