닭 췌장 Protein Methylase II의 분리정제 및 성질

• 영문명: Protein Methylase II from Chicken Pancreas: Purification and Properties
• 발행기관: 대한약학회
• 저자명: 유태무(Tae Moo Yoo) 남궁석민(Suck Min Namkoong) 홍성렬(Sung Youl Hong) 이향우(Hyang Woo Lee)
• 간행물 정보: 『약학회지』제35권 제6호 (1991년), 473~482쪽, 전체 10쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 1991.12.30

영문 초록

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.

키워드

Protein methylase Ⅱ non-denaturating gel electrophoresis hemoglobin pI Km Ki Vmax