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The isoenzyme forms of lactate dehydrogenase from the testes of Uromastix hardwickii
M H Javed1, M A Qureshi, M A Waqar
1Department of Biochemistry, Aga Khan University Medical College, Karachi, Pakistan.
Biochemistry and Molecular Biology International
|November 1, 1994
Abstract:
Lactate dehydrogenase was purified from testes of Uromastix hardwickii. The enzyme did not bind to DEAE-Sepharose at pH 7.2. A gel electrophoretic study of the crude enzyme showed the presence of three isoenzymes. The pH optima for pyruvate reduction and lactate oxidation were 7.0 and 9.5, respectively. The purified enzyme showed a single band after SDS-PAGE corresponding to a molecular weight of 34 KDa. The Km values for pyruvate, NADH, lactate and NAD+ were 0.019, 0.045, 9.0 and 0.011 mM, respectively. Pre-heating of the enzyme showed that it was stable up to 70 degrees C.