The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites |
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| Authors: | M S Rose and E A Lock |
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| Institution: | Biochemical Mechanisms Section, Medical Research Council Toxicology Unit, Woodmansterne Road, Carshalton, Surrey, U.K. |
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| Abstract: | 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. |
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