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Spectral and kinetic studies on the binding of trithiomolybdate to bovine and canine serum albumin in vitro the interaction with copper

, : Spectral and kinetic studies on the binding of trithiomolybdate to bovine and canine serum albumin in vitro the interaction with copper. Journal of Inorganic Biochemistry 30(4): 261-272

Spectral studies showed that copper and trithiomolybdate participated in a three-way interaction with bovine and canine serum albumin. The interaction with the proteins was affected by increased pH and ionic strength. Kinetic studies of binding equilibria indicated that [35S] trithiomolybdate bound to both albumins at a single site. The affinity of the site, but not the capacity of the protein, was increased by copper. It was concluded that the site was distinct from the N-terminal copper (and nickel) binding site, which is present on BSA but absent from CSA. Whether or not the N-terminal site has a role in copper transport is discussed. Reversible thiomolybdate-copper-protein interactions of this type may play a fundamental role in pathogenesis of Mo-induced syndromes, since as the normal binding patterns are perturbed the interprotein equilibria are altered and the copper distribution patterns are modified.

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Accession: 006459508

PMID: 3668523

DOI: 10.1016/0162-0134(87)80070-3

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