The dephosphorylation of inositol 1,4-bisphosphate to inositol in liver and brain involves two distinct Li+-sensitive enzymes and proceeds via inositol 4-phosphate
| Autor: | R. Baker, S Aspley, Robert J. Barnaby, R G Jackson, N S Gee, C I Ragan, K J Watling, D C Billington, Paul D. Leeson, G G Reid |
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| Rok vydání: | 1988 |
| Předmět: |
Inositol Phosphates
Phosphatase In Vitro Techniques Lithium Biochemistry Dephosphorylation Hydrolysis chemistry.chemical_compound Chlorides Animals Inositol Molecular Biology Chromatography High Pressure Liquid chemistry.chemical_classification Brain Cell Biology Phosphate Phosphoric Monoester Hydrolases Rats Enzyme Liver chemistry Sugar Phosphates Enantiomer Lithium Chloride Research Article |
| Zdroj: | Biochemical Journal. 249:143-148 |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | 1. Hydrolysis of both enantiomers of inositol 1-phosphate and both enantiomers of inositol 4-phosphate to inositol is inhibited by LiCl in liver and brain. 2. The phosphatase activity is predominantly soluble. 3. Inositol 1,4-bisphosphate is also hydrolysed by the soluble fraction of liver and brain. 4. Bisphosphatase activity is inhibited by LiCl, but is less sensitive than monophosphatase activity. 5. The product of bisphosphatase in liver and brain is inositol 4-phosphate. |
| Databáze: | OpenAIRE |
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