Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2.
Affiliation
Paterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester M20 9BXIssue Date
1976-11
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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.Citation
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 MedJournal
International Journal of Radiation Biology and Related Studies in Physics, Chemistry, and MedicineDOI
10.1080/09553007614551261PubMed ID
1087285Type
ArticleLanguage
enISSN
0020-7616ae974a485f413a2113503eed53cd6c53
10.1080/09553007614551261