Comparison of the ADH7 gene structure in caucasian and Japanese subjects

Hirokazu Yokoyama, Enrique Baraona, Charles S. Lieber

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The ADH 7 gene, encoding the σ-alcohol dehydrogenase isozyme, was cloned from a Caucasian genomic DNA library. Comparison of the nucleotide sequence of its exon 7 with that of an ADH 7 previously cloned from a Japanese subject revealed a substitution of the glycine-287 in the Caucasian σ isozyme with valine in the Japanese, Since a possible mutation at this site could account for ethnic differences in the gastric activity of this isozyme, the frequency of this change was examined in both races. The exon 7 of the ADH 7 was amplified by PCR from 7 Caucasian and 7 Japanese genomic DNA and applied to restriction fragment length polymorphism analysis, using Ava II to digest the sequence encoding glycine -287 and Mae III to digest that encoding valine-287. Regardless of ethnicity, all PCR amplicons were digested by Ava II and none by Mae III, suggesting that the ethnic difference in the 287 amino acid may represent an uncommon mutation, which does not account for the high frequency of minimal activity of the σ-alcohol dehydrogenase in the Japanese stomach compared to those of non-Orientals.

Original languageEnglish
Pages (from-to)875-878
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume212
Issue number3
DOIs
Publication statusPublished - 1995 Jan 1
Externally publishedYes

Fingerprint

Isoenzymes
Alcohol Dehydrogenase
Genes
Valine
Glycine
Exons
Stomach
Polymerase Chain Reaction
Mutation
Gene encoding
Genomic Library
Polymorphism
Gene Library
Restriction Fragment Length Polymorphisms
Substitution reactions
Nucleotides
Amino Acids
DNA

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Comparison of the ADH7 gene structure in caucasian and Japanese subjects. / Yokoyama, Hirokazu; Baraona, Enrique; Lieber, Charles S.

In: Biochemical and Biophysical Research Communications, Vol. 212, No. 3, 01.01.1995, p. 875-878.

Research output: Contribution to journalArticle

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