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The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites.


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.

SUBMITTER: Rose MS 

PROVIDER: S-EPMC1179579 | biostudies-other | 1970 Nov

REPOSITORIES: biostudies-other

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