Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2.
Eadsforth, C Power, D Thomas, E
Eadsforth, C
Power, D
Thomas, E
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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.
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1976-11
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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