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KMID : 0380219940270030179
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 3 p.179 ~ p.184
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Purification and Characterization of Protein Methylase II from Porcine Spleen
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Abstract
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Abstract:
@EN Protein methylase ll (S-adenosyl-L-methionine: protein O-methyltransferase. EC 2.1.1.24) was purified 692 fold with yield of 8.9% from porcine spleen by subcellular fractionation, pH treatment, ion exchange chromatography, gel filtration and
HPLC.
The purified enzyme gave a single band upon SDS-polyacrylamide gel electrophoresis. The molecular weight of purified protein metylase II was 40.700 daltons and the pl value was 7.4. The most effective substrates for porcine spleen protein
methylase
II
were myelin basic protein, followed by hemoglobin, histone, γ-globulin, gelain, cytochrome c, and serum albumin.
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