Premium
Evidence of hemoglobin dissociation
Author(s) -
Lunelli Lorenzo,
Zuliani Paola,
Baldini Giancarlo
Publication year - 1994
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360340607
Subject(s) - tetramer , dissociation (chemistry) , chemistry , hemoglobin , monomer , ionic bonding , chemical physics , crystallography , computational chemistry , ion , organic chemistry , polymer , enzyme
Bovine carbonmonoxy hemoglobin investigated with light scattering studies is found to dissociate from its native tetramer structure into dimers and monomers. The values of the hydrated tetramer radius, R T = 32.1 Å, and the fractional dissociation vs pH, have been obtained at different ionic strengths from the autocorrelation function of the scattered light. The results suggest that a relevant contribution to Hb dissociation is due to electrostatic effects and, by means of a model derived by Tanford, it has been possible to predict the behavior of dissociation. Among the findings of this approach, we recall the estimates of the electrostatic energy contributions to Hb dissociation, up to ≃ GRT, and the predicted charge of tetrameric Hb vs pH, which agrees very well with the experimental data. © 1994 John Wiley & Sons, Inc.