• Interactions of alkyl sulphates with bovine-serum albumin studied using eaq--as a probe.

      Eadsforth, C; Power, D; Thomas, E; Davies, J V (1977-03)
      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.
    • Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2.

      Eadsforth, C; Power, D; Thomas, E; Paterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester M20 9BX (1976-11)
      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.