- 영문명
- Protein Methylase Inhibitor from Porcine Liver: Purification and Properties
- 발행기관
- 대한약학회
- 저자명
- 박선미(Sun Mee Park) 박연호(Youn Ho Park) 백운기(Woon Ki Paik) 이향우(Hyang Woo Lee)
- 간행물 정보
- 『약학회지』제37권 제2호 (1993년), 149~157쪽, 전체 9쪽
- 주제분류
- 의약학 > 기타의약학
- 파일형태
- 발행일자
- 1993.04.30

국문 초록
영문 초록
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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