Abstract
The self-association of deoxyhemoglobin S was measured in dilute solutions (0 to 5 g/dl) by Rayleigh light scattering at 630 nm and osmometry in 0.05 M potassium phosphate buffer (pH 7.35). Weight and number average molecular weights (Mw and Mn, respectively) and the second or higher virial coefficients, B' were determined. No experimentally significant differences were observed between oxy- and deoxy-Hb S up to the concentration of 2 g/dl; their apparent average molecular weights were within experimental error. Above that concentration, both Mn and Mw of deoxy-Hb S were significantly different from that of oxy-Hb S. The negative second viral coefficent of deoxy-Hb S, observed by both techniques, is consistent with the self-association of this protein. The lack of effect of 0.4 M propylurea on the state of aggregation and the significant influence of 0.1 M NaCl suggests that polar interactions are involved in formation of these aggregates.
Highlights
University, The self-association of deoxyhemoglobin S was measured in dilute solutions (0 to 5 g/dl) by Rayleigh light scattering at 630 nm and osmometry in 0.05 M potassium phosphate buffer
No experimentally significant differences were observed between oxy- and deoxy-Hb S up to the concentration of 2 gldl; their apparent average molecular weights were within experimental error
The purpose of this paper is to analyze by osmometry and light scattering methods, low concentration
Summary
University, The self-association of deoxyhemoglobin S was measured in dilute solutions (0 to 5 g/dl) by Rayleigh light scattering at 630 nm and osmometry in 0.05 M potassium phosphate buffer (pH 7.35). No experimentally significant differences were observed between oxy- and deoxy-Hb S up to the concentration of 2 gldl; their apparent average molecular weights were within experimental error. That concentration, both M, and M, of deoxy-Hb S were significantly different from that of oxy-Hb S. The negative second virial coefficient of deoxy-Hb S, observed by both techniques, is consistent with the self-association of this protein.
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