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        돼지 간장 조직에서 얻은 단백질 메칠라제 저해제의 정제와 특성

        박선미(Sun Mee Park),박연호(Youn Ho Park),백운기(Woon Ki Paik),이향우(Hyang Woo Lee) 대한약학회 1993 약학회지 Vol.37 No.2

        Protein methylase inhibitor which is a modulator of biological methylation has been purified and characterized from porcine liver soluble fraction by cell fractionation, Sephadex G25 chromatography, reverse phase HPLC, size exclusion HPLC. The results are summarized as follows. 1) The purified inhibitor shows apparent homogeneity, as judged by HPLC. 2) A molecular weight of the purified inhibitor which is composed of 18 amino acid residues is about 1,400 daltons. 3) A single absorption peak of ultraviolet spectrum was observed at 260nm. 4) The inhibitor was not inactivated by heating at 100oC until 60min. and its activity was not influenced by treatment with digestive enzymes, such as trypsin, pepsin, pronase, chymotrypin, lysozyme, DNase, and RNase. 5) The purified inhibitor inhibited protein methylase I, II, III and phospholipid methyltransferase activities. 6) The purified inhibitor inhibited noncompetitively protein methylase II from porcine liver, spleen, and testis. 7) The Ki values for protein methylase II from porcine liver, spleen, and testis were 3OOnM, 25OnM, 297nM, respectively.

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