Elbaum D, Nagel R L, Herskovits T T
J Biol Chem. 1976 Dec 10;251(23):7657-60.
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.
在0.05 M磷酸钾缓冲液（pH 7.35）中，通过630 nm处的瑞利光散射和渗透压测定法，在稀溶液（0至5 g/dl）中测量脱氧血红蛋白S的自缔合。测定了重均分子量和数均分子量（分别为Mw和Mn）以及第二或更高维里系数B'。在浓度达到2 g/dl之前，未观察到氧合血红蛋白S和脱氧血红蛋白S之间有实验上的显著差异；它们的表观平均分子量在实验误差范围内。高于该浓度时，脱氧血红蛋白S的Mn和Mw均与氧合血红蛋白S有显著差异。通过两种技术观察到的脱氧血红蛋白S的负第二维里系数与该蛋白质的自缔合一致。0.4 M丙基脲对聚集状态没有影响，而0.1 M NaCl有显著影响，这表明极性相互作用参与了这些聚集体的形成。
