Abstract
In the present paper the ultracentrifugal, electrophoretic, and optical rotation behavior of apomyoglobin as a function of pH and ionic strength is reported. It has been observed that polymerization occurs between pH 3 and 5.5, with maximum association between pH 4 and 5. At pH 8, the isoelectric point of apomyoglobin I, no change in sedimentation coefficient with different ionic strengths was observed. In free electrophoresis at pH 5 and 0.1 ionic strength, only a single rather symmetric peak was seen. The rotatory dispersion constant decreases with a change of pH from 5 to 3, thus indicating an unfolding of the molecules at pH 3. The nature of the polymerization reaction is discussed.
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