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Evidence for dissociation of ferrihemoglobin by poly-L-lysine
Authors:K Imai  T Yoshimura
Institution:(1) Institute for Enzyme Research, Tokushima University, School of Medicine, 770 Tokushima, Japan;(2) Present address: Department of Biochemistry, Shimane Medical University, 693 Izumo-shi, Japan
Abstract:Summary Circular dichroism and absorption spectra of ferrihemoglobin were shown to be altered upon binding with poly-L-lysine at alkaline pH. When ferrihemoglobin immobilized to Sepharose gel was treated with poly-L-lysine, hemoglobin subunits were released from the gel. These results suggest that ferrihemoglobin was dissociated into subunits by poly-L-lysine.We thank Dr A. Ichihara and K. Aki for their valuable discussions and encouragement during the course of these studies.
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