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KMID : 0377519830080010097
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Chung-Ang Journal of Medicine
1983 Volume.8 No. 1 p.97 ~ p.106
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Purification and Characterization of Soluble form Trehalase from Rabbit Kidney
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Park Sei-Woong
Lee Dong-Wook
Lee Hi-Sung
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Abstract
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The purification and some properties of trehalase(α, α-trehalose 1-D-glucohydrolase, EC 3.2.1.28) in rabbit kidney has been studied. The activity of trehalase was measured by the method of lapp and mason. Soluble form trehalase was purified by ammonium sulfate precipitation, DEAE-cellulose and Sephadex G-200 column chromatography. The result obtained were as follows; 1. The activity of trehalase in rabbit kidney was 232 units/g. This enzyme was distributed in the cytosolic, mitochondrial and nuclei fraction. About 25% of the total activity was found in the cytosolic fraction. 2. The soluble form of trehalase was purified approximately 112-fold. 3. This enzyme was highly specific for trehalose as substrate. 4. The optimum pH of the trehalase was 6.0 in phosphate buffer. Acetate buffer, however, shifted the optimum pH to 5.2. 5. The optimal temperature of trehalase was 55℃. 6. The apparent molecular weight of the rurified enzyme was estimated to be 70,000 by Sephadex G-200 gel filtration.
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