and ionic strength 0.02, w = 0.065 in the native state and w = 0.023 in the expanded state. These values of w require that the configurational change, at this temperature and ionic strength, at pH 3.5, should be accompanied by the binding of 29 protons per 67,000 g. If allowance is made for the fact that the radius of the expanded form is probably larger at ionic strength 0.02 than at ionic strength 0.04 (cf. serum albumin5), then the calculated proton uptake is increased to about 34. It thus appears that most, and perhaps all of the observed uptake of 36 protons can be accounted for.Ferrihemoglobin used in this study was prepared from crystalline horse oxyhemoglobin (kindly furnished by Dr. J. H. Wang) by the method of Steinhardt and Zaiser.8 The author is indebted to Dr. E. P. Geiduschek and Mr. G. Saliba for invaluable assistance in performing these measurements.
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