Abstract
Hemoglobin was isolated from chicken blood and purified by biochemical methods.This hemoglobin was allowed to interact with copperglutathione (CuGSH) and the interaction pattern was monitored by spectrophotometric and spectrofluorimetric techniques. The interaction ratio was found to be 1:0.7 in both the cases. The equilibrium constant data suggested associative binding and a fluorimetric study revealed that such association occurred around tryptophan residues of hemoglobin.
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