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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0004927,
umls-concept:C0007452,
umls-concept:C0014063,
umls-concept:C0023688,
umls-concept:C0037506,
umls-concept:C0037633,
umls-concept:C0041213,
umls-concept:C0150312,
umls-concept:C0449432,
umls-concept:C1167622,
umls-concept:C1179435,
umls-concept:C1260956,
umls-concept:C1382100,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248
|
| pubmed:issue |
2
|
| pubmed:dateCreated |
1976-8-2
|
| pubmed:abstractText |
The interaction of the azo dye (2,3'-dimethyldiphenyl-7-azo-8-amino-1-napthol 3,6-disulfonic acid (TBR) and sodium dodecyl sulfate with the bovine myelin basic protein has been studied using absorbance, circular dichroism and 220 MHz PMR spectroscopy. Additional analyses of the binding reaction were carried out using light scattering, ultracentrifugal and electrophoretic techniques. A procedure for preparing pure TBR was developed. A modified structure for this synthesized TBR has been suggested. The mechanism of TBR binding to the myelin basic protein was found to be metachromatic. In addition, the interaction of TBR with the basic protein which gives rise to aggregation of the dye bound species was found to be analogous to the model proposed by Schwarz, G. and Seelig-Löffler, A. ((1975) Biochim. Biophys. Acta 379, 125-138) to explain the binding of acridine orange with poly (alpha-L-glutamic acid). PMR spectral analyses suggested that arginine residues provide the majority of primary sites of attachment on the basic protein for TBR. The effect of sodium dodecyl sulfate binding with the bovine myelin basic protein was found to induce a minimal change in the conformation of the protein. The induction of only about 20% alpha helial structure could be demonstrated and the binding was reversed by raising the solution temperature to 73 degrees C. The difference in the observed behavior of basic protein arising from TBR binding as opposed to the binding of sodium dodecyl sulfate is viewed as resulting from two different binding mechanisms. The binding behavior of TBR is primarily a consequence of charge-charge interaction while the binding effects of sodium dodecyl sulfate are a consequence of hydrophobic interaction. The sodium dodecyl sulfate binding acts as a shield which limits charge-charge interaction in the basic protein molecule thus preventing aggregate formation while TBR imposes no such restraints.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
14
|
| pubmed:volume |
427
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
392-409
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:57802-Animals,
pubmed-meshheading:57802-Binding Sites,
pubmed-meshheading:57802-Cattle,
pubmed-meshheading:57802-Circular Dichroism,
pubmed-meshheading:57802-Hydrogen-Ion Concentration,
pubmed-meshheading:57802-Kinetics,
pubmed-meshheading:57802-Ligands,
pubmed-meshheading:57802-Light,
pubmed-meshheading:57802-Magnetic Resonance Spectroscopy,
pubmed-meshheading:57802-Myelin Basic Proteins,
pubmed-meshheading:57802-Protein Binding,
pubmed-meshheading:57802-Protein Conformation,
pubmed-meshheading:57802-Scattering, Radiation,
pubmed-meshheading:57802-Sodium Dodecyl Sulfate,
pubmed-meshheading:57802-Solubility,
pubmed-meshheading:57802-Spectrophotometry,
pubmed-meshheading:57802-Spectrophotometry, Ultraviolet,
pubmed-meshheading:57802-Trypan Blue
|
| pubmed:year |
1976
|
| pubmed:articleTitle |
The solution behavior of the bovine myelin basic protein in the presence of anionic ligands. Binding behavior with the red component of trypan blue and sodium dodecyl sulfate.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|