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KMID : 0377519810060020205
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Chung-Ang Journal of Medicine
1981 Volume.6 No. 2 p.205 ~ p.215
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Studies on α-Glyecrophosphate Dehydrogenase from Ascaris Suum Muscle
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Joh Chang-Muk
Lee Hi-Sung
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Abstract
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The distribution and some properties of α-glycerophosphate dehydrogenase of Ascaris suum muscle has been studied. The activity of cytosolic NAD-linked α-glycerophosphate dehydrogenase (NAD 2-oxidoreductase, EC 1.1.1.8) was measured by the method of Gonzalez-Cerozo and Dalziel and the activity of FAD-linked α-glycerophosphate dehydrogenase (Cytochrome oxidoreductase, EC 1.1.99.5) was estimated according to the method of Swierczynski. The activity of NAD-linked dehydrogenase in homogenate was found to be 323 units per g wet tissue and was recovered about 61% in cytosolic fraction (specific activity: ca. 2.02). The activity of the FAD-linked dehydrogenase in homogenate was found to be 38.9 units per g and was recovered about 26% in mitochondria (specific activity; ca. 0.96). Thus, the specific activity of NAD-linked enzyme in cytosol was found to be about 2.1 fold greater than that of FAD-linked enzyme in mitochondria. The optimal pH for cytosolic NAD-linked enzyme was about 9.0 and the optimal temperature was 55℃. The Km values for sn-glycerol 3-phosphate and NAD’ were 4.5mM and 0.63mM, respectively. The present studies revealed that cytosolic NAD-linked α-glycerophosphate dehydrogenase has only one molecular form.
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