Linked Life Data

6529581

Source:http://linkedlifedata.com/resource/pubmed/id/6529581

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
1985-4-29
pubmed:abstractText
We have extended our previous theoretical analysis of the kinetics for radioactive GTP incorporation into steady-state microtubules [Zeeberg, B., Reid, R., & Caplow, M. (1980) J. Biol. Chem. 255, 9891-9899] to include the effects of a kinetic barrier for equilibration of labeled GTP with the tubulin E site. This binding has been found to be relatively slow; the half-time for GTP dissociation is approximately 25 s (k = 0.028 s-1). The slow binding of radioactive GTP apparently accounts for the following observations: (a) more radioactive nucleotide is incorporated into steady-state microtubules in the first 20 s when tubulin-[3H]GTP is used in a pulse than when [3H]GTP is used; (b) when steady-state microtubules are pulsed for 20 s with tubulin-[3H]GTP and then chased with excess nonradioactive GTP, radioactive nucleotide incorporation is not stopped immediately. Quantitative analysis of these results indicates that our steady-state microtubules do not contain significant amounts (greater than 1%) of GDP or GTP which can exchange with added GTP. The principal route for labeled nucleotide incorporation appears to be from tubulin-[3H]GTP subunit uptake, by diffusional and treadmilling processes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6745-52
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Mechanism for nucleotide incorporation into steady-state microtubules.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, U.S. Gov't, P.H.S.