Evidence for dissociation of ferrihemoglobin by poly-L-lysine.
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.
D002942:Circular Dichroism; D006801:Humans; D007700:Kinetics; D008706:Methemoglobin; D010108:Oxyhemoglobins; D010455:Peptides; D011107:Polylysine; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry
D010108:Oxyhemoglobins; D010455:Peptides; D011107:Polylysine; D008706:Methemoglobin