Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1976-7-6
pubmed:abstractText
1. Tubulin is not an adenosine-3':5'-monophosphate-dependent (cyclic-AMP-dependent) protein kinase. Both entities have been clearly separated by sucrose gradient ultracentrifugation. With a tubulin preparation obtained by the polymerization-depolymerization technique protein kinase had a sedimentation coefficient of 8.7 S whereas tubulin sedimented with 6.4 S. After preincubation with both cyclic AMP and histone the kinase dissociated into its catalytic subunit with a sedimentation coefficient of 3.4 S. 2. Tubulin prepared by the polymerization-depolymerization technique was neither phosphorylated in vivo nor in vitro. On the contrary if this preparation was further purified by the Weisenberg's procedure (DEAE-Sephadex batch absorption) before incubation with [gamma-32 P]ATP, phosphorylation occurred. Thus, phosphorylation depended on the method used to purify tubulin i.e. was likely to an an artefact.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
539-49
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Phosphorylation of microtubule-associated proteins.
pubmed:publicationType
Journal Article