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猪睾丸乳酸脱氢酶-C的cDNA克隆、表达酶的热稳定性及品系间多态性

cDNA cloning of pig testicular lactate dehydrogenase-C, thermal stability of the expressed enzyme, and polymorphism among strains.

作者信息

Huang H W, Liu T Z, Lee K H, Tu C F, Lee W C, Shimogiri T, Mannen H, Li S S

机构信息

Institute of Biomedical Sciences, National Sun Yat-Sen University, Taiwan, ROC.

出版信息

Gene. 2000 Jan 25;242(1-2):151-4. doi: 10.1016/s0378-1119(99)00532-6.

Abstract

Pig testicular lactate dehydrogenase-C (LDHC) cDNA was cloned and sequenced. The deduced sequence of 332 amino acids from pig LDHC shows 73% and 67% identity with that of pig LDHA (muscle) and LDHB (heart) respectively, whereas pig LDHA and LDHB isozymes shows 74% sequence identity. Pig and mouse LDHC cDNAs were subcloned into bacterial expression vector, and the expressed pig LDHC isozyme was shown to be as thermally stable as mouse LDHC isozyme. Pig genomic DNAs from Chinese Meishan, English Yorkshire, Danish Landrace and American Duroc were shown to exhibit polymorphic sites for restriction enzymes EcoRI, BamHI and PstI.

摘要

克隆并测序了猪睾丸乳酸脱氢酶-C(LDHC)的cDNA。从猪LDHC推导的332个氨基酸序列与猪LDHA(肌肉)和LDHB(心脏)的序列分别具有73%和67%的同一性,而猪LDHA和LDHB同工酶显示出74%的序列同一性。将猪和小鼠的LDHC cDNA亚克隆到细菌表达载体中,所表达的猪LDHC同工酶显示出与小鼠LDHC同工酶一样的热稳定性。来自中国梅山猪、英国约克夏猪、丹麦长白猪和美国杜洛克猪的猪基因组DNA显示,对于限制性内切酶EcoRI、BamHI和PstI存在多态性位点。

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