Sudo K, Maekawa M, Ikawa S, Machida K, Kitamura M, Li S S
Laboratory of Genetics, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709.
Biochem Biophys Res Commun. 1990 Apr 30;168(2):672-6. doi: 10.1016/0006-291x(90)92373-8.
A human lactate dehydrogenase-B mutant gene was isolated from a genomic DNA library constructed from a patient with unstable LDH-B (heart) subunit. The nucleotide sequences of seven protein-coding exons were determined and a single nucleotide substitution of G by A at Arg codon CGC in exon 4 was found. This mutation results in an amino-acid replacement of a conserved arginine by histidine at the residue "173," which is involved in an anion-binding site at the P-axis of LDH subunits.
从一名乳酸脱氢酶-B（心脏）亚基不稳定患者构建的基因组DNA文库中分离出一个人类乳酸脱氢酶-B突变基因。测定了7个蛋白质编码外显子的核苷酸序列，发现在外显子4中，精氨酸密码子CGC处的G被A单核苷酸取代。该突变导致在残基“173”处保守的精氨酸被组氨酸取代，该残基参与乳酸脱氢酶亚基P轴上的阴离子结合位点。
