title: Conformational changes induced by polyanions in haemoglobin from Camelus dromedarius. Studies on the ferric derivatives.
abstract: The effect of inositol hexakisphosphate on the redox equilibria and on the c.d. spectra of ferric derivatives of haemoglobin from Camelus dromedarius has shown that: two distinct functionally relevant binding sites for polyanions are present on the protein; conformational changes promoted by inositol hexakisphosphate are largely dependent on spin state of the iron; tertiary and quaternary changes are not necessarily linked; structures induced by polyanions can be mixed forms that are neither T-state nor R-state.
mesh_terms: D000818:Animals; D002162:Camelus / Q000097:blood*; D002942:Circular Dichroism; D005290:Ferric Compounds / Q000097:blood; D006454:Hemoglobins / Q000378:metabolism*; D007294:Inositol / Q000031:analogs & derivatives / Q000494:pharmacology; D008706:Methemoglobin / Q000031:analogs & derivatives; D000071228:Polyelectrolytes; D011108:Polymers / Q000494:pharmacology*; D011487:Protein Conformation / Q000187:drug effects
chemical_list: D005290:Ferric Compounds; D006454:Hemoglobins; D007294:Inositol; D008706:Methemoglobin; D000071228:Polyelectrolytes; D011108:Polymers; C013063:inositol hexasulfate