Literature DB >> 3338576

Absence of 7-acetyl taxol binding to unassembled brain tubulin.

M Takoudju1, M Wright, J Chenu, F Guéritte-Voegelein, D Guénard.   

Abstract

The effect of taxol on microtubule proteins at 0 degrees C is controversial. In order to determine if taxol is unable to bind to unassembled tubulin, as has been hypothesized, the binding of [3H]acetyl taxol has been studied using equilibrium microdialysis. Ac-taxol bound to microtubules at 37 degrees C and the binding remained stable when the temperature was lowered to 0 degrees C. Ac-taxol bound also at 0 degrees C to microtubules stabilized with rhazinilam. In contrast, there was no binding of Ac-taxol to unassembled tubulin, either free tubulin at 0 degrees C or tubulin, complexed with several microtubule poisons, at 0 and 37 degrees C.

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Year:  1988        PMID: 3338576     DOI: 10.1016/0014-5793(88)80875-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Demonstration of microtubule-like structures formed with (-)-rhazinilam from purified tubulin outside of cells and a simple tubulin-based assay for evaluation of analog activity.

Authors:  Michael C Edler; Guangli Yang; M Katherine Jung; Ruoli Bai; William G Bornmann; Ernest Hamel
Journal:  Arch Biochem Biophys       Date:  2009-06-02       Impact factor: 4.013

2.  Unique functional characteristics of the polymerization and MAP binding regulatory domains of plant tubulin.

Authors:  J D Hugdahl; C L Bokros; V R Hanesworth; G R Aalund; L C Morejohn
Journal:  Plant Cell       Date:  1993-09       Impact factor: 11.277

  2 in total

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