| pubmed-article:2845918 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2845918 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:2845918 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:2845918 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:2845918 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:2845918 | lifeskim:mentions | umls-concept:C0163342 | lld:lifeskim |
| pubmed-article:2845918 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2845918 | pubmed:dateCreated | 1988-11-21 | lld:pubmed |
| pubmed-article:2845918 | pubmed:abstractText | myo-Inositol-1-phosphatase from bovine brain was purified over 2000-fold. The native enzyme has a Mr of 59,000, and on SDS/polyacrylamide-gel electrophoresis the subunit Mr was 31,000. Thus the native enzyme is a dimer of two apparently identical subunits. The enzyme, purified to a specific activity of more than 300 units/mg of protein (1 unit of enzyme activity corresponds to the release of 1 mumol of Pi/h at 37 degrees C), catalysed the hydrolysis of a variety of phosphorylated compounds, the best one, in terms of V/Km, being D-myo-inositol 1-phosphate. Kinetic constants of compounds tested, including both isomers of glycerophosphate and two deoxy forms of beta-glycerophosphate, were measured. They show the importance of the two hydroxyl groups which are adjacent to the phosphate in myo-inositol 1-phosphate. With a wide variety of substrates Li+ was found to be an uncompetitive inhibitor whose Ki varied with substrate structure. | lld:pubmed |
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| pubmed-article:2845918 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2845918 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2845918 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2845918 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2845918 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:2845918 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2845918 | pubmed:author | pubmed-author:ChanalM CMC | lld:pubmed |
| pubmed-article:2845918 | pubmed:author | pubmed-author:DucepJ BJB | lld:pubmed |
| pubmed-article:2845918 | pubmed:author | pubmed-author:AttwoodP VPV | lld:pubmed |
| pubmed-article:2845918 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2845918 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2845918 | pubmed:volume | 253 | lld:pubmed |
| pubmed-article:2845918 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2845918 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2845918 | pubmed:pagination | 387-94 | lld:pubmed |
| pubmed-article:2845918 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2845918 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2845918 | pubmed:articleTitle | Purification and properties of myo-inositol-1-phosphatase from bovine brain. | lld:pubmed |
| pubmed-article:2845918 | pubmed:affiliation | Merrell Dow Research Institute, Strasbourg, France. | lld:pubmed |
| pubmed-article:2845918 | pubmed:publicationType | Journal Article | lld:pubmed |
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