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
dc.contributor.author | Liebes, Leonard F. | en_US |
dc.contributor.author | Zand, Robert | en_US |
dc.contributor.author | Phillips, William D. | en_US |
dc.date.accessioned | 2006-04-07T16:29:24Z | |
dc.date.available | 2006-04-07T16:29:24Z | |
dc.date.issued | 1976-04-14 | en_US |
dc.identifier.citation | Liebes, Leonard F., Zand, Robert, Phillips, William D. (1976/04/14)."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." Biochimica et Biophysica Acta (BBA) - Protein Structure 427(2): 392-409. <http://hdl.handle.net/2027.42/21790> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GJ-47S63CR-3D/2/1cbd6b0ba6e148abf474d9c8a14642c6 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/21790 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=57802&dopt=citation | en_US |
dc.description.abstract | The interaction of the azo dye (2,3'-dimethyldiphenyl-7-azo-8-amino-l-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-Loffler, A. (1975) Biochim. Biophys. Acta 379,125-138) to explain the binding of acridine orange with poly([alpha]--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[deg]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. | en_US |
dc.format.extent | 853669 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | 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 | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Biophysics Research Division and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48105 and Central Research Department, E. I. du pont de Nemours and Co., Wilmington, Del. 19899, U.S.A. | en_US |
dc.contributor.affiliationum | Biophysics Research Division and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48105 and Central Research Department, E. I. du pont de Nemours and Co., Wilmington, Del. 19899, U.S.A. | en_US |
dc.contributor.affiliationum | Biophysics Research Division and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48105 and Central Research Department, E. I. du pont de Nemours and Co., Wilmington, Del. 19899, U.S.A. | en_US |
dc.identifier.pmid | 57802 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/21790/1/0000185.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2795(76)90184-7 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.