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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


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

Accession: 006459508

PMID: 3668523

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

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