• YAKHAK HOEJI
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• v.38 no.5
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• pp.608-613
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• 1994

We isolated two Cd-binding high molecular weight proteins from intraperitoneally cadmium injected rat liver. Molecular weight of Cd-BP(I) purified from Sephacryl S-100 and DEAE Sepharose column chromatography and Cd-BP(II) purified from DEAE Sepharose column chromatography and Sulphonyl Sepharose column chromatography was 33,000 and 18,400, respectively. Alcohol dehydrogenase and alkaline phosphatase acitivities were not detected from two purified proteins.

• Korean journal of applied entomology
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• v.34 no.3
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• pp.181-190
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• 1995

Malate dehydrogenase in the mosquito ovary after a blood meal, Aedes aegypti, was purified and characterized. MDH purification steps involved DEAE-Sepharose, S-Sepharose and Cibacron blue affinity chromatography. The purified MDH was 70,000 daltons in molecular weight and was a homodimer consisting of tow identical subunits. Optimal activity of purified MDH was obtained pH 9.0-9.2 in malate-oxaloacetate reaction and pH 9.8-10.2, in oxaloactate-malate reaction. With obtained pH 9.0-92 in malate-oxaloacetate reaction and pH 9.8-10.2, in oxaloactate-malate reaction. With malate as substrate, purified mitochondrial MDH (1.28$\times$${10}^{-4}$ M) had lower Km value than cytoplasmic MDH (8.92x${10}^{-3}$ M). MDH activity was inhibited by citrate, $\alpha$-ketoglutarate, and ATP. Inhibition of MDH activity by ATP and citrate was less in malate-oxaloacetate reaction and in oxaloacetate-malate reaction. MDH activity was completely inhibited by ATP in oxaloacetate-malate reaction and not inhibited by citrate in malate-oxaloacetate reaction. Temporal activity change of MDH is similar to that of isocitrate dehydrogenase in the ovary after blood feeding; their activities in the ovary began to rise at 18 hours after a blood meal, and reached at the maximal level at 48 hours.