Document Detail


The association between phosphatidylinositol phosphodiesterase activity and a specific subunit of microtubular protein in rat brain.
MedLine Citation:
PMID:  4353236     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
P J Quinn
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  133     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1973 Jun 
Date Detail:
Created Date:  1973-10-11     Completed Date:  1973-10-11     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  273-81     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
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:
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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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