The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites
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A protein fraction was isolated from guinea-pig liver that binds triethyltin with an affinity of approx. 2×106m−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.
1962 ◽
Vol 40
(1)
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pp. 983-987
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1989 ◽
Vol 180
(1)
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pp. 161-166
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1988 ◽
Vol 263
(28)
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pp. 14296-14301
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1986 ◽
Vol 35
(24)
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pp. 4387-4393
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1962 ◽
Vol 40
(8)
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pp. 983-987
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