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

Submission Date :
9 / 11 / 2006 , 10 : 49 : 56
Abstract Number :
Presenting Type:
Poster Presentation
Presenting Area :
Authors :
이지은, 김미희, 정제훈
전남대학교 화학과,
Assigned Code :
28P278포 Assigend Code Guideline
Presenting Time :
금 <발표Ⅱ>
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.