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      • KCI등재

        단백질 메틸화효소류 및 S-아데노실-L-메치오닌 연결효소의 활성도에 미치는 사염화탄소-유발 간독서의 영향

        남궁석민(Suck Min Namkoong),유태무(Tae Moo Yoo),홍성렬(Sung Youl Hong),이향우(Hyang Woo Lee) 대한약학회 1992 약학회지 Vol.36 No.1

        In order to test relationships between hepatotoxicity and transmethylation, activities of protein methylases and SAM (S-adenosyl-L-methionine)-synthetase wee examined in liver tissues of rats treated with CCl4. Also the concentrations of SAM and SAH were measured by HPLC in rat liver. The results are as follows. (1). Activities of protein methylases were not significantly changed in 24 hours after CCl4 treatment. However, in 48 hours, activities of protein methylases were significantly increased in comparison with that of control. (2). Activity of SAM-synthetase was increased steadily in the time course after CCl4 treatment.(3). S-adenosyl-L-methionine concentration of liver tissues in CCl4-treated group was elevated in 24 hours, and then decline thereafter. But the SAH concentration was slightly decreased in the time course after CCl4 treatment. These results indicated that SAM was very actively used in transmethylation reactions of CCl4 damaged rat liver, suggesting the strong relationships between hepatotoxicity and transmethylation phenomena.

      • KCI등재

        닭 췌장 Protein Methylase II의 분리정제 및 성질

        유태무(Tae Moo Yoo),남궁석민(Suck Min Namkoong),홍성렬(Sung Youl Hong),이향우(Hyang Woo Lee) 대한약학회 1991 약학회지 Vol.35 No.6

        Protein methylase II (S-adenosyl-L-methionine:protein carboxyl-0-methyltransferase; EC 2.1.1.24., PM II) was purified from chicken pancreas by subcellular fractionation, DEAE-cellulose chromatography, QAE-Sephadex A-50 chromatography, Sephadex G-75 chromatography, and Sephadex G-75 rechromatography. The purified PM II gave a single band upon polyarcrylamide gel electrophoresis both in the presence of SDS and in Tris glycine buffer without SDS. The pI value of purified PM II was identified as 5.7 on isoelectric focusing gel. Properties and activities of PM II were studied and the following results were obtained. 1) PM II from chicken pancreas was purified approximately 221-fold with a yield of 1.3%. 2) The purified PM II appear constituted of a single polypeptide chain of a molecular weight 46,800 daltons. 3) Hemoglobin exhibited the highest of methyl-accepting activity among the substrates tested. 4) The purified PM II has a Km of 4.67 X 10-6M and a Vmax of 37.5 pmoles of methyl-14C/min/mg enzyme for SAM-14CH3 as methyl donor in the presence of histone type II-As. 5) It is found that S-adenosyl-L-homocysteine is a competitive inhibitor for PM II with KI value of 3.23 X 10-5M.

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