BMB Reports
- Volume 31 Issue 3
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- Pages.274-280
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- 1998
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- 1976-670X(eISSN)
Rat Duodenal Mucosa Inositol Monophosphatase; Novel Enzyme of Which Properties are Distinct from Brain Enzyme
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Kwon, Hyeok-Yil
(Department of Physiology, College of Medicine, Hallym University) ;
- Lim, Bong-Hee (Department of Physiology, College of Medicine, Hallym University) ;
- Park, Hyung-Seo (Department of Physiology, College of Medicine, Hallym University) ;
- Lee, Yun-Lyul (Department of Physiology, College of Medicine, Hallym University) ;
- Lee, Eun-Hee (Department of Genetic Engineering, Division of Life Sciences, Hallym University) ;
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Choi, Soo-Young
(Department of Genetic Engineering, Division of Life Sciences, Hallym University) ;
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Park, Hyoung-Jin
(Department of Physiology, College of Medicine, Hallym University)
- Received : 1998.02.16
- Published : 1998.05.31
Abstract
An inositol monophosphatase (IMPase) was purified to homogeneity from rat duodenal mucosa for the first time and its enzymatic properties were investigated. Rat duodenal mucosa peculiarly exhibited the highest IMPase activity among various rat tissues examined. By means of ammonium sulfate precipitation, followed by Q-Sepharose, polylysine agarose, reactive-red agarose column chromatography, Uno-Q FPLC, and Bio-Silect FPLC, duodenal IMPase was purified 223-fold to a specific activity of 13.6 U/mg protein. The molecular mass of the native enzyme was estimated to be 48,000 Da on gel filtration. The subunit molecular mass was determined by SDS-PAGE to be 24,000 Da. These results indicate that duodenal IMPase is a dime ric protein made up of identical subunits. Rat duodenal IMPase has distinct properties from brain IMPase. It has a broad spectrum of substrate specificity and is insensitive to