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Three single nucleotide polymorphisms leading to non‐synonymous amino acid substitution in the human ribonuclease 2 and angiogenin genes exhibit markedly less genetic heterogeneity in six populations
Author(s) -
Ueki Misuzu,
Takeshita Haruo,
Fujihara Junko,
Takatsuka Hisakazu,
Yuasa Isao,
Iida Reiko,
Yasuda Toshihiro
Publication year - 2008
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.1498
Subject(s) - angiogenin , single nucleotide polymorphism , genetics , biology , snp genotyping , rnase p , genotype , gene , snp , genotyping , polymorphism (computer science) , population , microbiology and biotechnology , rna , medicine , environmental health , angiogenesis
Angiogenin and ribonuclease 2 (RNase 2) are members of the human RNase superfamily. Although three potential single nucleotide polymorphisms (SNPs) in these genes, which could give rise to an amino acid substitution in the protein, have been identified, relevant population data are not available, and accordingly they have not been applied to clinical–genetic analysis. For this purpose, a novel genotyping method for each SNP using the mismatched PCR‐restriction fragment length polymorphism technique has been developed. Using this method, the genotype distribution of each SNP was investigated in six populations: Japanese ( n = 167), Korean ( n = 90), Mongolian ( n = 92), Ovambos ( n = 86), Turkish ( n = 87), and German ( n = 70). In all the populations, only one genotype was found in each SNP. Irrespective of differences in ethnic groups, the angiogenin and RNase 2 genes appear to exhibit markedly less genetic heterogeneity with regard to these SNPs. Copyright © 2008 John Wiley & Sons, Ltd.