Binding of a denatured heme protein and ATP to erythroid spectrin.

@article{Chakrabarti2001BindingOA,
  title={Binding of a denatured heme protein and ATP to erythroid spectrin.},
  author={Abhijit Chakrabarti and Shekhar Bhattacharya and Sibnath Ray and Malyasri Bhattacharyya},
  journal={Biochemical and biophysical research communications},
  year={2001},
  volume={282 5},
  pages={
          1189-93
        }
}
Spectrin is a large, worm-like cytoskeletal protein that is abundant in all cell types. The denatured heme enzyme, horseradish peroxidase showed significant decrease in the reactivation yield, after 30 min of refolding, in presence of increasing concentrations of spectrin from that in the absence. This indicated that spectrin could bind denatured HRP and inhibit their refolding. In presence of 1 mM ATP and 10 mM MgCl(2) the spectrin binding of denatured HRP is abolished. This activity of… CONTINUE READING
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