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돼지 간장 조직내 Protein Methylase Ⅱ 저해제의 정제 및 특성
권명희,정기경,이회영,이향우,홍성렬 ( Myung Hee Kwon,Ki Kyung Jung Hoi,Young Lee,Hyang Woo Lee,Sungyoul Hong ) 생화학분자생물학회 1994 BMB Reports Vol.27 No.6
An inhibitor for protein methylase II (EC 2.1.1.24) was solubilized from porcine liver microsomal fraction by heat treatment, and purified by ultrafiltration, Sephadex G-25 chromatogrnphy, and HPLC using μ-Bondapak C_(18) column. The purified inhibitor was near homogeniety as judged by HPLC. The molecular weight of the inhibitor was estimated to be 1,676 Da by analysis of amino acid composition. And it was revealed that the inhibitor molecule is rich in alanine and glycine. The activity of the inhibitor was not affected by heat treatment up to 100℃ as well as hydrolytic enzymes. The K; value for the protein methylase II which has been purified from porcine spleen was measured to be 1.3 × 10^(-7) M. Inhibition studies showed that the inhibitor was noncompetitive with respect to S-adenosyl-L-methionine (SAM) and activities of several SAM-dependent methylases were also inhibited by the purified inhibitor.