The photochemical binding of bithionol to soluble proteins and peptides.
The photochemical reactions of the bacteriocide bithionol (a known photoallergen in man) with soluble proteins and peptides, were investigated. Solutions of human serum albumin (HSA), human gamma-globulin, bovine insulin and poly-L-lysine were irradiated with ultraviolet light of wavelength 313 nm in the presence of [35S]-bithionol and the extent of photochemical (covalent) binding determined. HSA bound at least four molecules of bithionol per molecule of HSA. Bithionol was also found to bind to gamma-globulin to a similar extent; lower levels of binding were achieved with bovine insulin and poly-L-lysine. A bithionol-HSA photoadduct was treated with cyanogen bromide to determine the selectivity of binding. Fractionation after cyanogen bromide treatment showed that bithionol was bound to both major fragments of HSA, with a preference for the N-terminal region of the protein.
Delahanty
J N
JN
Department of Chemistry and Applied Chemistry, University of Wales, College of Cardiff, U.K.
Evans
J C
JC
Rowlands
C C
CC
Pendlington
R U
RU
Barratt
M D
MD
D001735:Bithionol / Q000032:analysis*; D003488:Cyanogen Bromide; D006801:Humans; D010455:Peptides / Q000032:analysis*; D010636:Phenols / Q000032:analysis*; D010777:Photochemistry; D011485:Protein Binding; D011506:Proteins / Q000032:analysis*; D012709:Serum Albumin / Q000032:analysis; D012995:Solubility; D014466:Ultraviolet Rays; D005719:gamma-Globulins / Q000032:analysis
D010455:Peptides; D010636:Phenols; D011506:Proteins; D012709:Serum Albumin; D005719:gamma-Globulins; D001735:Bithionol; D003488:Cyanogen Bromide