Abstract
Eye-specific lactate dehydrogenase (EC 1.1.1.27, LDH) 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 isozyme was 154.8 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal pH for enzymatic reaction of the eye-specific LDH isozyme was pH 8.5. value of the purified eye-specific LDH isozyme was M using pyruvate as a substrate. These results indicate that we must consider pH when measuring eye-specific LDH isozyme activity. The eye-specific LDH isozyme had a higher binding affinity for the substrate as a pyruvate than LDH A4 isozyme. Antibodies produced against the purified eye-specific LDH isozyme may be used in the diagnosis of several human diseases and in comparative physiological studies of fishes.
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