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KMID : 0366919920040010024
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Sungkyun Pharmceutical Journal
1992 Volume.4 No. 1 p.24 ~ p.33
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Protein Methylase II from Hog Pancreas: Purification and Properties
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Lee Hyang-Woo
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Abstract
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Protein methylase II(S-adenosyl-L-methionine: protein carboxyl-O-methyltransferase; EC 2.1.1.24., PM II) was partially purified from hog pancreas by subcellular fractionation, DEAE-cellulose chromatography, SAH-sepharose 4B chromatography and
Sephadex
G-75 chromatography. The properties and activities of PM II were studied and the following results were obtained.
1) PM II was purified approximately 235-fold with a yield of 12.5%.
2) The purified enzyme was appeared to be constituted of a single polypeptide chain of a molecular weight 24,000 daltons.
3) The purified enzyme showed a broad specificity for substrates.
4) The purified enzyme has a Km of 4×10-6M and a Vmax of 75.2 pmoles of methyl-14C/min/mg enzyme for SAM-14CH3 as methyl donor in the presence of histone type II-As.
5) It was found that S-adenosyl-L-homocysteine was a competitive inhibitor for PM II with Ki value of 5×10-5M.
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