Evidence for dissociation of ferrihemoglobin by poly-L-lysine

descriptionPublicationkeyboard_double_arrow_right Article 01 Aug 1979 English Publisher:Springer Science and Business Media LLCJournal:Experientia, volume 35, pages 1,003-1,005 (issn: 0014-4754, eissn: 1420-9071,

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Authors: K, Imai; T, Yoshimura;

doi: 10.1007/bf01949906

pmid: 477855

Evidence for dissociation of ferrihemoglobin by poly-L-lysine

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Abstract

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.

Related Organizations

University of Tokushima
Japan

Keywords

Kinetics, Protein Conformation, Spectrophotometry, Circular Dichroism, Oxyhemoglobins, Humans, Polylysine, Peptides, Methemoglobin, Protein Binding

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