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

  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},
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. 

Human δ-aminolevulinate dehydratase: chromosomal localization to 9q34 by in situ hybridization

Southern blot analysis of somatic cell hybrids informative for ALA-D was consistent and supported the finding of only one locus for this heme biosynthetic enzyme.

δ-Aminolevulinate dehydratase: Induced expression and regional assignment of the human gene to chromosome 9q13»qter

Examination of secondary, tertiary, and quaternary XX-8 subclones revealed that the expression of the human isozyme segregated with human chromosome 9q, confirming the provisional regional assignment made by classical linkage studies.

Hereditary hepatic porphyria with delta aminolevulinate dehydrase deficiency: Immunologic characterization of the non-catalytic enzyme

The molecular basis that accounts for the deficiency of ALA-D in these patients is a structurally modified enzyme, found by using two different immunologic methods to find a cross-reactive immunologic material (CRIM+) which corresponded to 20% and 33% of the control level.

Comparative map for mice and humans

This report summarizes the status of this comparative map and provided a listing of homologous genes and anonymous loci that have been mapped in mice and humans together with references documenting homology and the chromosomal and linkage assignments.

Fragile X frequency in a mentally retarded population in Brazil.

The estimated frequency of Martin-Bell [fra(X)] syndrome among mentally impaired individuals in Brazil was similar to that previously reported in other countries.



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.