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Purification and characterization of lactate dehydrogenase from Varanus liver
Experimental & Molecular Medicine ; : 25-30, 1997.
Article in English | WPRIM | ID: wpr-179548
ABSTRACT
Lactate dehydrogenase was purified 21-fold from liver of Varanus bengalensis using colchicine-sepharose column chromatography. The crude enzyme showed two isoenzymes (LDH-5 and LDH-4) by agarose gel electrophoresis (AGE). The purified enzyme showed a single band after SDS-PAGE corresponding to molecular mass of 35 kDa. The molecular mass of native enzyme was about 140 kDa. The optimum pH for the forward reaction was 7.5 while that for the reverse reaction was pH 9.5. The K-m values for pyruvate, NADH, lactate and NAD(+) were 0.17 +/- 0.037, 0.02 +/- 0.004, 12.4 +/- 3.05 and 0.38 +/- 0.032 mM, respectively. Pre-heating of enzyme showed that its t(50) was 40-50 degrees C. Oxalate and n-hexanediol were inhibitors for both forward and reverse reactions. Among divalent ions, Cu++ was shown to be more effective inhibitor for the forward reaction.
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Full text: Available Index: WPRIM (Western Pacific) Main subject: Chromatography / Lactic Acid / Pyruvic Acid / Electrophoresis, Agar Gel / Electrophoresis, Polyacrylamide Gel / Hydrogen-Ion Concentration / Ions / Isoenzymes / L-Lactate Dehydrogenase / Liver Language: English Journal: Experimental & Molecular Medicine Year: 1997 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Chromatography / Lactic Acid / Pyruvic Acid / Electrophoresis, Agar Gel / Electrophoresis, Polyacrylamide Gel / Hydrogen-Ion Concentration / Ions / Isoenzymes / L-Lactate Dehydrogenase / Liver Language: English Journal: Experimental & Molecular Medicine Year: 1997 Type: Article