Purification and properties of inositol-1,4-bisphosphatase from bovine brain
| Autor: | C I Ragan, Robert J. Barnaby, R G Jackson, G G Reid, N S Gee |
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| Rok vydání: | 1988 |
| Předmět: |
Tris
Ion chromatography Lithium Biochemistry Potassium Chloride Substrate Specificity Hydrolysis chemistry.chemical_compound Animals Magnesium Inositol Molecular Biology Magnesium ion chemistry.chemical_classification Gel electrophoresis Chromatography biology Brain Cell Biology Hydrogen-Ion Concentration Phosphoric Monoester Hydrolases Kinetics Enzyme chemistry Enzyme inhibitor biology.protein Cattle Electrophoresis Polyacrylamide Gel Chromatography Liquid Research Article |
| Zdroj: | Biochemical Journal. 253:777-782 |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | Inositol-1,4-bisphosphatase has been purified 13,000-fold from bovine brain supernatant. The enzyme is monomeric, with an apparent subunit Mr of 40,000. Maximal hydrolytic rates were observed in Tris buffer, pH 7.8, in the presence of 9 mM-Mg2+. The enzyme acted as a 1-phosphatase, hydrolysing both inositol 1,4-bisphosphate [Ins(1,4)P2] (Km 0.04 mM) and inositol 1,3,4-trisphosphate [Ins(1,3,4)P3] (Km 0.5 mM) to inositol 4-phosphate and inositol 3,4-bisphosphate respectively. Li+ inhibited the hydrolysis of both substrates in an uncompetitive manner, with apparent Ki values of 9.63 mM and 0.46 mM for Ins(1,4)P2 and Ins(1,3,4)P3 respectively. |
| Databáze: | OpenAIRE |
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