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KMID : 0613820140240020118
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Journal of Life Science
2014 Volume.24 No. 2 p.118 ~ p.127
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Kinetic Properties of Lactate Dehydrogenase in Tissues from Rana catesbeiana
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Yum Jung-Joo
Ha Eun-Sung
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Abstract
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The kinetic properties and isozyme expression of lactate dehydrogenase (EC 1.1.1.27; LDH) in tissues from Rana catesbeiana I and II collected from February (I) and August (II) were studied. LDH activities, A4 isozyme, and LDH/citrate synthase (EC 4.1.3.7; CS) were high in skeletal muscle from R. catesbeiana I, and LDH B₄ isozyme increased in several tissues of R. catesbeiana II. In particular, LDH activities were high in heart and brain tissues from R. catesbeiana II. LDH eye-specific C isozyme, detected by native polyacrylamide gel electrophoresis after immunoprecipitation, was expressed in eye tissue and was more similar to the B₄ than A₄ isozyme. LDH A₄ isozyme was purified by oxamate-linked affinity chromatography, and the molecular weight of subunit A was 32.0 kDa. In R. catesbeiana II, levels of Km^PYU, Vmax^LAC, and tolerance to lactate of LDH were high in all tissues, and Vmax^PYU of LDH in heart and brain tissue was highly detected. Purified A₄ isozyme and LDH in eye tissue were highly tolerate compared to others. The Km^LAC value was highly measured compared to Km^PYU. The degree of inhibition by 10 mM of pyruvate on LDH activities in tissues from R. catesbeiana I and II was more pronounced as the ratio of subunit B increased. As a result, characteristic expression of LDH eye-specific C was found in R. catesbeiana. Anaerobic metabolism seemed to predominate as the LDH of skeletal muscle from I showed higher activity. It also appeared that R. catesbeiana II adapted well to incremental increases in LDH B, becoming tolerant to the lactate of LDH in tissues.
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KEYWORD
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Citrate synthase, Km, lactate dehydrogenase, LDH-eye-specific C isozyme, Rana catesbeiana
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