Linked Life Data

3768342

Source:http://linkedlifedata.com/resource/pubmed/id/3768342

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1986-12-15
pubmed:abstractText
Tubulin purified from calf brain cytoplasm, normally a compact water-soluble dimer, is able to interact with the mild detergents octyl glucoside (a minimum of 60 detergent molecules) and deoxycholate (95 +/- 8 molecules). Binding is cooperative and approaches saturation below the critical micelle concentration of the amphiphiles. Binding is accompanied by a quenching of the intrinsic protein fluorescence, but no spectral shape changes indicating denaturation such as in the case of sodium dodecyl sulfate are observed. Glycerol, which is known to be preferentially excluded from the tubulin domain and to favor the folded and associated forms of this protein, inhibits the binding of the mild detergents. Octyl glucoside induces a rapidly equilibrating tubulin self-association reaction characterized by a bimodal sedimentation velocity profile with boundaries at approximately 5 and 12 S. Full dissociation of this detergent restores the normal sedimentation behavior to 90% of the protein. Binding of deoxycholate slows the sedimentation velocity of tubulin from s(0)20,w = 5.6 +/- 0.2 S to s(0)20,w = 4.8 +/- 0.3 S. Measurements of the molecular weight of the tubulin-deoxycholate complex indicate an increase from 100,000 to 143,000 +/- 5,000. The diffusion rate consistently decreases from (5.3 +/- 0.5) X 10(-7) to (3.8 +/- 0.2) X 10(-7) cm2 S-1. This is most simply interpreted as an expansion of the undissociated tubulin dimer upon detergent binding (a change in the frictional ratio, f/f min, from 1.35 to 1.86). It is concluded that tubulin shows a reversible transition between the water-soluble state and amphipathic detergent-bound forms which constitute a model system of tubulin-membrane interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5220-30
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Interaction of tubulin with octyl glucoside and deoxycholate. 1. Binding and hydrodynamic studies.
pubmed:publicationType
Journal Article