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dc.contributor.authorEadsforth, C
dc.contributor.authorPower, D
dc.contributor.authorThomas, E
dc.date.accessioned2011-11-25T15:12:51Z
dc.date.available2011-11-25T15:12:51Z
dc.date.issued1976-11
dc.identifier.citationInvestigation 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 Meden
dc.identifier.issn0020-7616
dc.identifier.pmid1087285
dc.identifier.doi10.1080/09553007614551261
dc.identifier.urihttp://hdl.handle.net/10541/190836
dc.description.abstractThe 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.isoenen
dc.subject.meshHumans
dc.subject.meshProtein Binding
dc.subject.meshPulse Radiolysis
dc.subject.meshSerum Albumin
dc.subject.meshSerum Albumin, Bovine
dc.subject.meshSulfuric Acids
dc.subject.meshThiocyanates
dc.titleInvestigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2.en
dc.typeArticleen
dc.contributor.departmentPaterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester M20 9BXen
dc.identifier.journalInternational Journal of Radiation Biology and Related Studies in Physics, Chemistry, and Medicineen
html.description.abstractThe 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.


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