title: Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin.
abstract: The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopic (absorbance, circular dichroism, EPR) properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin was investigated. The results obtained show that: (i) all polyanions bind to the protein at the same sites, but with different affinities; (ii) polyanions affect the protein conformation of the ferrous nitrosyl derivative in a different way with respect to aquo-ferric and ferrous oxy dromedary hemoglobin; and (iii) the data obtained provide further independent evidence for the existence in dromedary hemoglobin of two functionally distinct polyanion binding sites that affect the conformational equilibrium of the protein in opposite ways.
authors: Department of Biochemical Sciences, University of Rome La Sapienza, Italy.
authors: P
authors: P
authors: Ascenzi
authors: R
authors: R
authors: Santucci
authors: A
authors: A
authors: Desideri
authors: G
authors: G
authors: Amiconi
mesh_terms: D019794:2,3-Diphosphoglycerate; D000818:Animals; D000838:Anions; D001665:Binding Sites; D002162:Camelus / Q000097:blood*; D002942:Circular Dichroism; D016264:Dextran Sulfate; D003911:Dextrans / Q000494:pharmacology; D004163:Diphosphoglyceric Acids / Q000494:pharmacology; D004578:Electron Spin Resonance Spectroscopy; D006454:Hemoglobins / Q000378:metabolism*; D006493:Heparin / Q000494:pharmacology; D009569:Nitric Oxide / Q000097:blood*; D010833:Phytic Acid / Q000494:pharmacology; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry
chemical_list: D000838:Anions; D003911:Dextrans; D004163:Diphosphoglyceric Acids; D006454:Hemoglobins; D019794:2,3-Diphosphoglycerate; D009569:Nitric Oxide; D010833:Phytic Acid; D006493:Heparin; D016264:Dextran Sulfate