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dc.contributor.authorSchilstra, M.
dc.contributor.authorMartin, S.R.
dc.contributor.authorBayley, P.M.
dc.identifier.citationSchilstra , M , Martin , S R & Bayley , P M 1987 , ' On the relationship between nucleotide hydrolysis and microtubule assembly : Studies with a GTP-regenerating system ' , Biochemical and Biophysical Research Communications , vol. 147 , no. 2 , pp. 588-595 .
dc.identifier.otherPURE: 98366
dc.identifier.otherPURE UUID: 01640559-e914-4fad-a0f9-e858fb029aca
dc.identifier.otherdspace: 2299/3899
dc.identifier.otherScopus: 0023656098
dc.descriptionOriginal article can be found at: Copyright Elsevier Inc. [Full text of this article is not available in the UHRA]
dc.description.abstractThe assembly of pure tubulin dimer has been studied in two buffer systems (containing low and high glycerol/Mg), using a regeneration system protocol to assess the amount of GDP-tubulin in the assembling polymer. For both assembly systems studied, the GDP content is effectively stoichiometric with tubulin throughout assembly. This indicates a high degree of coupling between assembly and GTP-hydrolysis, giving a hydrolysis rate at least 10-fold faster than previously deduced. The steady state GTP hydrolysis rate is quantitatively consistent with this finding. We conclude that the extent of any GTP-tubulin cap is below the detectable limit, both during elongation and at steady state. MT-protein; microtubule protein; MAPs; microtubule associated proteins; PC-tubulin; tubulin dimer from phosphocellulose chromatography; GTP- and GDP-tubulin denotes the nucleotide at the exchangeable nucleotide binding site (E-site)RS; enzymic GTP-regenerating system.en
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.titleOn the relationship between nucleotide hydrolysis and microtubule assembly : Studies with a GTP-regenerating systemen
dc.contributor.institutionSchool of Computer Science
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Computer Science
rioxxterms.typeJournal Article/Review

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