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

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 LD...

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Bibliographic Details
Published in:Gene 2000-01, Vol.242 (1), p.151-154
Main Authors: Huang, H.-W., Liu, T.-Z., Lee, K.-H., Tu, C.-F., Lee, W.-C., Shimogiri, T., Mannen, H., Li, S.S.-L.
Format: Article
Language:English
Subjects:
Animals
DNA - genetics
DNA, Complementary - chemistry
DNA, Complementary - genetics
Enzyme Stability
Gene Expression
Genes - genetics
Hot Temperature
Isoenzymes
L-Lactate Dehydrogenase - genetics
L-Lactate Dehydrogenase - metabolism
lactate dehydrogenase
lactate dehydrogenase-A
lactate dehydrogenase-B
lactate dehydrogenase-C
Male
Mice
Molecular Sequence Data
Polymorphism, Genetic
Polymorphism, Restriction Fragment Length
Porcine
Protein sequence
Restriction sites
Sequence Analysis, DNA
Species Specificity
Swine
Temperature
Testis - enzymology
Thermal stability
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Summary: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.
ISSN:0378-1119
1879-0038
DOI:10.1016/S0378-1119(99)00532-6