Abstract
The specific Kerr constant of rabbit skeletal light meromyosin was measured in various buffer systems between pH 8.7 and 9.6 using transient electric birefringence and showed the generally expected decrease with solution conductivity. Analysis of birefringence rise times and held reversal transients showed that this decrease was connected with large changes in what appeared to be a permanent dipole moment. Comparison of the data with some theoretical predictions (O'Konski, C. T.; Krause, S. J. Phys. Chem. 1970, 74, 3243) indicated that the changes in the specific Kerr constant were most probably due to a slow induced dipole moment resulting from ion atmosphere polarization
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