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

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

*此作品的通信作者

研究成果: 期刊稿件文章同行評審

1 引文 斯高帕斯(Scopus)

摘要

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. (C) 2000 Elsevier Science B.V. All rights reserved.

原文英語
頁(從 - 到)151-154
頁數4
期刊Gene
242
發行號1-2
DOIs
出版狀態已出版 - 25 01 2000
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