Exonic point mutations in NADH-cytochrome B5 reductase genes of homozygotes for hereditary methemoglobinemia, types I and III: Putative mechanisms of tissue-dependent enzyme deficiency
| Autor: | Katsube, Takanori, Sakamoto, Norihiro, Kobayashi, Yasushi, Seki, Ritsuko, Hirano, Masami, Tanishima, Kiyoh, Tomoda, Akio, Takazakura, Eisuke, Yubisui, Toshitsugu, Takeshita, Masazumi, Sakaki, Yoshiyuki, Fukumaki, Yasuyuki |
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| Jazyk: | angličtina |
| Rok vydání: | 1991 |
| Předmět: |
Adult
Male Base Sequence Protein Conformation Homozygote Molecular Sequence Data Chromosome Mapping Original Articles Exons Polymerase Chain Reaction Deoxyribonuclease HpaII Introns Mutation Humans Deoxyribonucleases Type II Site-Specific Methemoglobinemia Cytochrome Reductases Cytochrome-B(5) Reductase |
| Popis: | We analyzed the NADH-cytochrome b5 reductase gene of hereditary methemoglobinemia type I and type III, by using PCR-related techniques. The mutation in type I is a guanine-to-adenine substitution in codon 57 of exon 3 of the NADH-cytochrome b5 reductase gene, and the sense of this codon is changed from arginine to glutamine. In type III the mutation is a thymine-to-cytosine transition in codon 148 of exon 5, causing leucine-to-proline replacement in type III. The former mutation abolishes the MspI recognition site. Homozygosity for the former mutation in a patient with type I was confirmed by restriction analysis of PCR-amplified fragments and by dot blot hybridization of amplified products with allele-specific oligonucleotide probes. The latter mutation generates a recognition site for MspI. Amplification of exon 5 by PCR followed by digestion with MspI revealed homozygosity for this mutation in patients with type-III. Putative mechanisms of tissue-dependent enzyme defects in hereditary methemoglobinemia are discussed. |
| Databáze: | OpenAIRE |
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