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08월 30일 20시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능
Inorganic pyrophosphatase : a heat-stable protein in
Submission Date :
9 / 11 / 2006 , 10 : 49 : 56
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The soluble inorganic pyrophosphatase (PPase) from
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
Has an Increased Thermostability ”, Biochemistry,
, 1531-1536), the PPase activity in this study was not affected by heat treatment. The crude extract from
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
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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