Abstract
The lactate dehydrogenase (EC 1.1.1.27, LDH) isozyme in skeletal muscle of mandrin fish (Siniperca scherzeri) was successfully purified by affinity chromatography and ultrafiltration. The molecular weight of the purified LDH isozyme was 140.4 kDa and its isoelectric point (pI) was 7.0. Optimal pH for enzymatic reaction was 7.5. and value of the purified LDH isozyme were M and 13.31 mM/min using pyruvate as a substrate, respectively. These kinetic properties of the purified LDH isozyme supported the fact that the mandrin fish was a warm-adapted species. The antibody against the purified LDH isozyme may be used in the metabolic physiological studies of ectothermic vertebrates and in the diagnosis of several human diseases.
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