Multiplicity of different stable quaternary conformations in ferric hemoglobin from Camelus dromedarius. Modulation by small anions.
The effect of small anions in modulating polyphosphate-induced conformational changes in ferric dromedary hemoglobin (Camelus dromedarius) was investigated. The results obtained indicate that: i) in solution, the simultaneous presence of polyphosphate and small anions is essential to obtain quaternary changes in the protein; ii) the charge, rather than the size or sterical configuration, mainly affects the quaternary structural equilibrium of the macromolecule; iii) three distinct, stable quaternary conformers of ferric dromedary hemoglobin were detected spectroscopically as a function of charge and concentration of small anion.
Santucci
R
R
Dipartimento di Scienze Biochimiche, Università La Sapienza, Roma.
Amiconi
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G
D000818:Animals; D000838:Anions; D002162:Camelus / Q000097:blood*; D002712:Chlorides / Q000494:pharmacology; D002942:Circular Dichroism; D006454:Hemoglobins / Q000378:metabolism*; D010833:Phytic Acid / Q000494:pharmacology; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet
D000838:Anions; D002712:Chlorides; D006454:Hemoglobins; D010833:Phytic Acid