Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2.
dc.contributor.author | Eadsforth, C | |
dc.contributor.author | Power, D | |
dc.contributor.author | Thomas, E | |
dc.date.accessioned | 2011-11-25T15:12:51Z | |
dc.date.available | 2011-11-25T15:12:51Z | |
dc.date.issued | 1976-11 | |
dc.identifier.citation | Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2. 1976, 30 (5):449-57 Int J Radiat Biol Relat Stud Phys Chem Med | en |
dc.identifier.issn | 0020-7616 | |
dc.identifier.pmid | 1087285 | |
dc.identifier.doi | 10.1080/09553007614551261 | |
dc.identifier.uri | http://hdl.handle.net/10541/190836 | |
dc.description.abstract | The reaction of the radical anion -(SCN)2-, produced during pulse radilysis of aqueous KCNS solutions, have been used to study the binding of a range of alkyl sulphates to bovine (BSA) and human (HSA) serum albumin. At neutral pH, -(SCN)2- reacts chiefly with trytophan residues. Approximately ten high-affinity binding sites are detectable for compounds of chain length greater than C7. The results are interpreted in terms of a model in which one hydrophobic region in the protein, containing the tryptophan residues, can accommodate the ten ligand molecules. Electrostatic interactions with positively-charged groups surrounding the hydrophobic area are also involved in binding. | |
dc.language.iso | en | en |
dc.subject.mesh | Humans | |
dc.subject.mesh | Protein Binding | |
dc.subject.mesh | Pulse Radiolysis | |
dc.subject.mesh | Serum Albumin | |
dc.subject.mesh | Serum Albumin, Bovine | |
dc.subject.mesh | Sulfuric Acids | |
dc.subject.mesh | Thiocyanates | |
dc.title | Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2. | en |
dc.type | Article | en |
dc.contributor.department | Paterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester M20 9BX | en |
dc.identifier.journal | International Journal of Radiation Biology and Related Studies in Physics, Chemistry, and Medicine | en |
html.description.abstract | The reaction of the radical anion -(SCN)2-, produced during pulse radilysis of aqueous KCNS solutions, have been used to study the binding of a range of alkyl sulphates to bovine (BSA) and human (HSA) serum albumin. At neutral pH, -(SCN)2- reacts chiefly with trytophan residues. Approximately ten high-affinity binding sites are detectable for compounds of chain length greater than C7. The results are interpreted in terms of a model in which one hydrophobic region in the protein, containing the tryptophan residues, can accommodate the ten ligand molecules. Electrostatic interactions with positively-charged groups surrounding the hydrophobic area are also involved in binding. |