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KMID : 0613820040140040708
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Journal of Life Science
2004 Volume.14 No. 4 p.708 ~ p.715
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Characterization and Evolutionary Relationship of Lactate Dehydrogenase in Liver of Lampetra japonica and Liver-specific C4 Isozyme in Gadus macrocephalus
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Park Sun-Young
Cho Sung-Kyu
Yum Jung-Joo
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Abstract
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The lactate dehydrogenase (EC 1.1.1.27,LDH) in liver of Lempetra japonica was purified in buffer of affinity chromatography. The liver-specific C4 isozyme of Gadus macrocephalus was purified by heat treatment, affinity chromatography, and DEAE-Sephacel chromatography. The liver-specific C4 isozyme was eluted in a buffer containing NAD+ and was coeluted with B4 isozyme in plain buffer of affinity chromagraphy. Liver-specific C4 isozyme in G. macrocephalus was the most thermostable, and B4 isozyme was more stable than A4. The LDH in the fraction of pH 7.45 purified from the liver of L. japonica by chromatofocusing was more inhibited by pyruvate than purified LDH. The optimum pH of the LDH isozyme in the liver of L. japonica was 7.5 and that of liver-specific C4 isozyme was 8.5. The LDH in liver of L. japonica made complexes more with antibody against Coreoperca herzi A4 and liver-specific C4 than with that against eye-specific C4. Therefore, the structure of the LDH in liver of L. japonica might be similarly evolved to that of subunit A and liver-specific C4 isozyme in liver tissue of G. macrocephalus. The evolution rate of subunit C is faster than that of subunit A. LDH in liver of L. japonica has not one isozyme but isozymes and it was also found out to have not only subunit A and B but also subunit C.
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KEYWORD
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lactate dehydrogenase, Lampetra japonica, Gadus macrocephalus, liver-specific C4 isozyme
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