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KMID : 0364219890320040420
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Korean Journal of Zoology
1989 Volume.32 No. 4 p.420 ~ p.428
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Purification, Kinetics and Immunochemistry of Two Homotetrameric Lactate Dehydrogenase Isozymes in Pseudogobio esocinlus (Cypriniformes)
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Kim Myong-Ock
Yum Jung-Joo
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Abstract
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Three tissues of heart, kidney and liver of a primitive cvprinid Pseudogobio esocinus were found to have lactate dehydrogenase isozyme(5) containing subunit C. Tissue expressions of genes for subunits A and B were similar to those of mammalian species. Molecular weight of the isozymes were estimated to be 140,000 approximately. Affinity chromatography of the isozymes on the immobilized oxamate gel revealed that A4 isozyme was not elected in NAD+ but in column buffer. B4 isozune was isozpnatically purified by subjecting kidney extract to a CM-Sepharose column. Ae isozvme as well as B4 isozvme was inhibited by high concentrations of pyruvate. The affinity chromatographic behavior and susceptibility to pyruvate inhibition of the A4 isorpne suggest that A4 isozwne is similar to B4 isozyme kinetically. Antibodies against p. esocinus A4 isogyme reacted with mouse At isozyme but not with p. esocinus B4 isogyme, reflecting that subunit B is less conservative in its evolution.
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KEYWORD
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Cypriniformes , Lactate dehydrogenase , Subunit C , Oxamate gel , Pyruvate in-gibition , Evolution rate
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