Assignment of the human gene for δ aminolevulinate dehydrase to chromosome 9 by somatic cell hybridization and specific enzyme immunoassay

@article{Beaumont1984AssignmentOT,
  title={Assignment of the human gene for $\delta$ aminolevulinate dehydrase to chromosome 9 by somatic cell hybridization and specific enzyme immunoassay},
  author={Carole Beaumont and Chantal Foubert and Bernard Grandchamp and Dominique Weil and V C N'guyen and M. S. Gross and Yves Nordmann},
  journal={Annals of Human Genetics},
  year={1984},
  volume={48}
}
A non‐competitive enzyme immunoassay specific for δ aminolevulinate dehydrase has been devised and applied to rodent–human hybrid cell lines. Two different conditions have been used, one specific for the human enzyme and the other indicative of both rodent and human enzymes. The ratio of the values obtained under the two conditions was used to discriminate between positive and negative clones. By this method the gene for ALA dehydrase has been assigned to chromosome 9. 

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References

SHOWING 1-10 OF 19 REFERENCES

δ‐aminolevulinate dehydrase: a new genetic polymorphism in man

A method has been developed for the electrophoretic and quantitative analyses of human red cell δ‐aminolevulinate dehydrase (ALADH), under the control of an autosomal gene, with two common codominant alleles with frequencies of 0–89 and Oil, respectively.

Inherited deficiency of delta-aminolevulinic acid dehydratase.

Intial experiments support the hypothesis that the mutation in this family with an inherited deficiency of red cell ALA-D activity occurring over three generations may affect a regulatory gene, but enzyme purification and further study are required.

Δ‐Aminolevulinatedehydrase: synteny with ABO‐AK1‐ORM (and assignment to chromosome 9)

A material comprising 846 normal families from the Copenhagen area was tested for δ‐aminolevulinatedehydrogenase and the most likely sequence, as judged from male θ values, was found to be ABO‐AK1 ‐ALADH‐ORM.

Production of mammalian somatic cell hybrids by means of polyethylene glycol treatment

Polyethylene glycol is very effective in producing hybrids capable of indefinite multiplication even in cases, such as early passage human skin fibroblasts and lymphocytes, known to be highly recalcitrant to other treatments.

Improved techniques for the induction of mammalian cell hybridization by polyethylene glycol

There is a marked effect of PEG concentration on cell hybridization, and there seem to be inherent differences between cells in terms of the extent of cell fusion induced by PEG.

Enzyme immunoassay ELISA and EMIT.