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dc.contributor.authorEadsforth, C
dc.contributor.authorPower, D
dc.contributor.authorThomas, E
dc.contributor.authorDavies, J V
dc.date.accessioned2011-08-08T12:20:19Z
dc.date.available2011-08-08T12:20:19Z
dc.date.issued1977-03
dc.identifier.citationInteractions of alkyl sulphates with bovine-serum albumin studied using eaq--as a probe. 1977, 31 (3):257-64 Int J Radiat Biol Relat Stud Phys Chem Meden
dc.identifier.issn0020-7616
dc.identifier.pmid300728
dc.identifier.doi10.1080/09553007714550301
dc.identifier.urihttp://hdl.handle.net/10541/139099
dc.description.abstractThe reactions of hydrated electrons produced during pulse radiolysis habe been used to investigate the binding of a range of alkyl sulphates to bovine-serum albumin. Binding to ten high-affinity sites is detectable for all compounds (methyl, hexyl, octyl, decyl, and dodecyl sulphates) studied. Sodium dodecyl sulphate, in contrast to the other analogues, causes large increases in the reactivity of BSA as a result of further binding. Possible mechanisms for this increase are discussed.
dc.language.isoenen
dc.subject.meshFatty Alcohols
dc.subject.meshProtein Binding
dc.subject.meshPulse Radiolysis
dc.subject.meshSerum Albumin, Bovine
dc.subject.meshSodium Dodecyl Sulfate
dc.titleInteractions of alkyl sulphates with bovine-serum albumin studied using eaq--as a probe.en
dc.typeArticleen
dc.identifier.journalInternational Journal of Radiation Biology and Related Studies in Physics, Chemistry, and Medicineen
html.description.abstractThe reactions of hydrated electrons produced during pulse radiolysis habe been used to investigate the binding of a range of alkyl sulphates to bovine-serum albumin. Binding to ten high-affinity sites is detectable for all compounds (methyl, hexyl, octyl, decyl, and dodecyl sulphates) studied. Sodium dodecyl sulphate, in contrast to the other analogues, causes large increases in the reactivity of BSA as a result of further binding. Possible mechanisms for this increase are discussed.


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