Linked Life Data

2730883

Source:http://linkedlifedata.com/resource/pubmed/id/2730883

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-7-27
pubmed:abstractText
The maximum achievable tyrosination level of neurotubulin, in vitro, is about 50%. We have developed a method to obtain a complete separation of the tyrosinatable and nontyrosinatable species. We use an immunoaffinity column, with coupled YL 1/2 monoclonal antibody (anti-Tyr-tubulin) and rapid desalting methods. Both subpopulations can be obtained in a polymerizable, apparently native, form. We find that about 35% of the brain tubulin is truly nontyrosinatable, despite the fact that it is assembly competent. Using a polyclonal antibody directed against nontyrosinatable tubulin, we find that it recognizes a specific epitope on the alpha-subunit of the dimer. The existence of an abundant tubulin subspecies, structurally different from tyrosinatable tubulin, should obviously be kept in mind in immunofluorescence studies of the distribution of nontyrosinated tubulin in brain tissues. Furthermore, we have extensively investigated the effect of tubulin tyrosination on microtubule dynamics. Despite the homogeneity of the populations under comparison, we find no significant effect of tyrosination on microtubule dynamics. Similarly, the stabilizing effects of microtubule associated proteins and of STOP protein were identical in both subpopulations. The drug taxol seems more efficient in stabilizing detyrosinated microtubules, but the difference is moderate. Taken together, these findings suggest that tubulin tyrosination does not effect microtubule stabilization, neither through modifications of the intrinsic tubulin properties nor through a differential binding of stabilizing proteins. Finally, the complete separation of two tubulin species (tyrosinated or detyrosinated) with similar kinetic properties, but immunologically different, should be of value in many kinetic studies of microtubule assembly.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2698-704
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affinity chromatography.
pubmed:affiliation
Laboratoire BRCE, INSERUM U 244, Centre d'Etudes Nucléaires, Grenoble, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't