Abstract
The decrease in oxygen affinity with increasing hemoglobin concentration, which occurs in solutions of pure hemoglobin S, can be used to determine the minimum concentration at which polymerization of the deoxy form takes place. On this basis a very sensitive method for measuring the minimum gelling concentration has been developed. The influence of temperature, pH, and other hemoglobins on the end points obtained by this method is described. In all cases excellent agreement with the minimum gelling concentration determined directly on larger samples was observed. The results of this investigation demonstrate that the decrease in oxygen affinity of red cells containing hemoglobin S with increasing intracorpuseular hemoglobin concentration [May, A., and Huehns, E. R. (1975) Brit. J. Haematol. 30, 317] is a direct consequence of the gelling properties of hemoglobin S alone.
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