Influence of protein-bound copper (II) on properties of bovine serum albumin-tryptophan complex (original) (raw)

Abstract

The influence of bound copper(II) on binding capabilities of tryptophan (Trp) and tyrosine (Tyr) to bovine serum albumin (BSA) was studied by means of equilibrium dialysis and ultrafiltration. The number of bound tryptophan increased in the presence of copper(II), coordinated to serum albumin, from 6.87 to 17.16 mols of Trp pro mole of bovine serum albumin in equilibrium studies and from 0.17 to 1.50 in ultrafiltration studies. Tyrosine was found inactive with BSA and BSA-Cu(II) complex.

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