The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites.
A protein fraction was isolated from guinea-pig liver that binds triethyltin with an affinity of approx. 2x10(6)m(-1) at pH8.0. It was shown that the protein responsible for binding 70% of the triethyltin found in guinea-pig liver after injection of radioactively labelled triethyltin is at most a few per cent of the total liver protein. Evidence is presented from the kinetics of loss of binding and loss of certain amino acids on photo-oxidation with either Methylene Blue or Rose Bengal that each binding site consists of two histidine residues.
D000818:Animals; D001665:Binding Sites; D002498:Centrifugation; D006168:Guinea Pigs; D006639:Histidine / Q000032:analysis*; D006358:Hot Temperature; D007093:Imidazoles; D007700:Kinetics; D008027:Light; D008099:Liver / Q000032:analysis*; D008297:Male; D008751:Methylene Blue; D008956:Models, Chemical; D008961:Models, Structural; D009942:Organometallic Compounds; D010084:Oxidation-Reduction; D010777:Photochemistry; D011485:Protein Binding; D011506:Proteins / Q000032:analysis; D011868:Radioisotopes; D012395:Rose Bengal; D014001:Tin
D007093:Imidazoles; D009942:Organometallic Compounds; D011506:Proteins; D011868:Radioisotopes; D012395:Rose Bengal; D006639:Histidine; D014001:Tin; D008751:Methylene Blue