Binding of triethyltin to cat haemoglobin and modification of the binding sites by diethyl pyrocarbonate

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Triethyltin binding to cat haemoglobin. Evidence for two chemically distinct sites and a role for both histidine and cysteine residues.

Triethyltin binding to cat haemoglobin was measured after pretreatment of the protein with diethyl pyrocarbonate at pH 6.0,iodoacetamide or phenylmercuric acetate or by photo-oxidation in the presence of Methylene Blue. The pentaco-ordinate nature of the binding of triethyltin to cat haemoglobin is confirmed by the inability of intramolecularly pentaco-ordinate tin compounds to compete. Conside...

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Reaction of 3-isothiocyanatonaphthalene-1,5-disulphonate with amino acids, peptides, and proteins [proceedings].

Phenylarsenious acid and diethyltin, which are known to have a great affinity for dithiol groups (Aldridge & Cremer, 1955; Peters, 1946), would be expected to compete with triethyltin for the two cysteine components of the triethyltin-binding sites. This was observed, although the affinities obtained with phenylarsenious acid and diethyltin for untreated cat haemoglobin (2x 1 0 4 ~ ' and approx...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1977

ISSN: 0264-6021

DOI: 10.1042/bj1630583