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Inorganic pyrophosphatase : a heat-stable protein in E. coli

등록일
2006년 9월 11일 10시 49분 56초
접수번호
1292
발표코드
28P278포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
이지은, 김미희, 정제훈
전남대학교 화학과,
The soluble inorganic pyrophosphatase (PPase) from E. coli hydrolyzes inorganic pyrophosphate to phosphate. It is an essential enzyme and plays an important role in the “phosphate cycle”. Although it was reported previously that PPase was labile in heat treatment (Takanori Satoh, Yoshimasa Takahashi, Noriko Oshida, Atsushi Shimizu, Hiroshi Shinoda, Machiko Watanabe, and Tatsuya Samejima (1999), “A Chimeric Inorganic Pyrophosphatase Derived from Escherichia coli and Thermus thermophilus Has an Increased Thermostability ”, Biochemistry, 38, 1531-1536), the PPase activity in this study was not affected by heat treatment. The crude extract from E. coli was fractionated by MonoQ ion-exchange chromatography and the PPase activity was separated as a single peak. The fraction containing the PPase activity was diluted 10 times and exposed to 95 ℃ for 5 minutes. The recovery of the PPase activity was 100 %. When the crude extract from E. coli was directly exposed to the same condition, the recovery was only 30 %. Co- precipitation of PPase with other denatured proteins seemed to cause the lower recovery.

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