| The association between phosphatidylinositol phosphodiesterase activity and a specific subunit of microtubular protein in rat brain. | |
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MedLine Citation:
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PMID: 4353236 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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1. Supernatant proteins from rat brain were separated into two fractions containing phosphatidylinositol phosphodiesterase activity by chromatography on DEAE-Sephadex A-50. 2. The first fraction sediments in linear sucrose density gradients in two bands corresponding to molecular weights of 66000 and 36000. There was presumptive evidence that the lighter protein constituted the monomeric form of the enzyme. The second fraction sediments predominantly as a single protein of molecular weight 86000. 3. Treatment of rat brain supernatant with [(3)H]colchicine abolished the second DEAE-Sephadex peak and removed the lighter protein from the first peak. These proteins emerged in the same position as the protein binding [(3)H]colchicine at high salt concentration; phospholipase activity was recovered from linear sucrose density gradients in positions corresponding to molecular weights 88000 and 43000, together with an aggregate of molecular weight 140000. Electrophoresis on sodium dodecyl sulphate-urea-polyacrylamide gels of this fraction revealed only three proteins: the alpha and beta-subunits of microtubular protein, of molecular weights 56000 and 52000 respectively, and a protein of molecular weight 38000. 4. A sample of microtubular protein from mouse, labelled in vivo with [(3)H]proline and (32)P(i), was added to rat brain supernatant together with an equal amount of the same microtubular protein treated with cyclic AMP and [gamma-(32)P]ATP and the mixture subsequently characterized by ion-exchange chromatography. Some phospholipase activity characteristic of the second peak from DEAE-Sephadex was associated with one fraction of added microtubular protein. This fraction was identified on the basis of the (3)H:(32)P ratio as the beta subunit of the protein treated with ATP and cyclic AMP. The subunit of added microtubular protein untreated with nucleotides was not associated with phospholipase activity. |
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Authors:
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P J Quinn |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: The Biochemical journal Volume: 133 ISSN: 0264-6021 ISO Abbreviation: Biochem. J. Publication Date: 1973 Jun |
Date Detail:
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Created Date: 1973-10-11 Completed Date: 1973-10-11 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 273-81 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Binding Sites Brain / cytology, enzymology* Centrifugation, Density Gradient Chromatography, Ion Exchange Chromatography, Thin Layer Colchicine / metabolism Electrophoresis, Polyacrylamide Gel Mice Microtubules / enzymology* Molecular Weight Nerve Tissue Proteins / isolation & purification, metabolism* Phosphatidylinositols Phosphoric Diester Hydrolases / isolation & purification, metabolism* Phosphorus Isotopes Proline Protein Binding Rats Sodium Dodecyl Sulfate Solubility Spectrophotometry, Ultraviolet Tritium |
| Chemical | |
Reg. No./Substance:
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0/Nerve Tissue Proteins; 0/Phosphatidylinositols; 0/Phosphorus Isotopes; 10028-17-8/Tritium; 147-85-3/Proline; 151-21-3/Sodium Dodecyl Sulfate; 64-86-8/Colchicine; EC 3.1.4.-/Phosphoric Diester Hydrolases |
| Comments/Corrections | |
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