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KMID : 0370219870310030173
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Yakhak Hoeji
1987 Volume.31 No. 3 p.173 ~ p.181
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Purification and Properties of Protein Methylase I from Hog Pancreas
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이향우/Lee HW
장만식/Chang MS
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Abstract
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Protein methylase I has been partially purified from hog pancreas with a 11% yeild. The final preparation is completely free of any other protein-specific methyltransferases and endogenous substrate proteins. The enzyme has an optimum pH of 7.2 and the approximate molecular weight is above 800 thousands dalton. The Km values for S-adenosyl-L-methionine and histone type II-A are 1.32 X 10-5M. The Ki value for S-adenosyl-L-homocysteine is 1.52 X 10-6M. The effect of enyzme concentration on the activity showed a slight sigmoidal curve suggesting the involvement of certain cofactors. Even though the purified enzyme showed two bands on polyacrylamide gel eiectrophoresis, the enzyme is highly specific for the arginine residues of protein and specifically, highly specific for histone, suggesting histonespecific protein methylase I .
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KEYWORD
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