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KMID : 0613820110210111565
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Journal of Life Science
2011 Volume.21 No. 11 p.1565 ~ p.1572
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Purification and Characterization of Eye-Specific Lactate Dehydrogenase C4 Isozyme in Greenling (Hexagrammos otakii)
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Cho Sung-Kyu
Yum Jung-Joo
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Abstract
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Eye-specific lactate dehydrogenase (EC 1.1.1.27, LDH) C₄ isozyme in the eyes of greenlings (Hexagrammos otakii) was successfully purified by affinity chromatography and continuous-elution electrophoresis. The molecular weight of the purified eye-specific LDH C₄ isozyme was 154.8 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal pH for enzymatic reaction of the eye-specific LDH C₄ isozyme was pH 8.5. K^{PYR}_m value of the purified eye-specific LDH C₄ isozyme was 1.88×10^{-5} M using pyruvate as a substrate. These results indicate that we must consider pH when measuring eye-specific LDH C₄ isozyme activity. The eye-specific LDH C₄ isozyme had a higher binding affinity for the substrate as a pyruvate than LDH A4 isozyme. Antibodies produced against the purified eye-specific LDH C₄ isozyme may be used in the diagnosis of several human diseases and in comparative physiological studies of fishes.
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KEYWORD
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Greenling (Hexagrammos otakii), lactate dehydrogenase (LDH), eye-specific LDH C₄ isozyme
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