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http://dx.doi.org/10.5352/JLS.2004.14.4.708

Characterization and Evolutionary Relationship of Lactate Dehydrogenase in Liver of Lampetra japonica and Liver-specific C4 Isozyme in Gadus macrocephdus.  

박선영 (동신제약 중앙연구소)
조성규 (청주대학교 생명유전통계학부 생명과학전)
염정주 (청주대학교 생명유전통계학부 생명과학전공)
Publication Information
Journal of Life Science / v.14, no.4, 2004 , pp. 708-715 More about this Journal
Abstract
The lactate dehydrogenase (EC 1.1.1.27, LDH) in liver of Lempetra japonica was purified in buffer of affinity chromatography. The liver-specific $C_4$ isozyme of Gadus macrocephalus was purified by heat treatment, affinity chromatography, and DEAE-Sephacel chromatography. The liver-specific $C_4$ isozyme was eluted in a buffer containing NAD+ and was coeluted with $B_4$isozyme in plain buffer of affinity chromagraphy. Liver-specific $C_4$ isozyme in G. macrocephalus was the most thermostable, and$B_4$isozyme was more stable than $A_4$. The LDH in the fraction of pH 7.45 purified from the liver of L. iaponica 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$C_4$ isozyme was 8.5. The LDH in liver of L. japonica made complexes more with antibody against Coreoperca herzi$A_4$ and liver-specific $C_4$ than with that against eye-specific $C_4$. Therefore, the structure of the LDH in liver of L. japonica might be similarly evolved to that of subunit A and liver-specific $C_4$ 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.
Keywords
lactate dehydrogenase; Lampetra iaponica; Gadus macrocephalus; liver-specific$C_4$isozyme.;
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