Interactions of alkyl sulphates with bovine-serum albumin studied using eaq--as a probe.
The 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.
D005233:Fatty Alcohols; D011485:Protein Binding; D011675:Pulse Radiolysis; D012710:Serum Albumin, Bovine; D012967:Sodium Dodecyl Sulfate
D005233:Fatty Alcohols; D012710:Serum Albumin, Bovine; D012967:Sodium Dodecyl Sulfate