In the previous paper (1), it was reported that Take-amylase A (TAA) has ten atoms of calcium per molecule, and one of them is essential for maintaining the active configuration of TAA. This conclusion was based on the fact that the elimination of the last calcium atom from the TAA molecule by the treatment with ethylenediamine tetraacetic acid (EDTA) caused an increase of levo-rotatory power of this protein. The optical rotatory power, however, is supposed to be affected by environmental conditions in addition to the intrinsic helical configuration of protein molecule. Thus, it is interesting to examine the rotatory dispersion which is an excellent measure for estimating the degree of folding of protein molecules. The present paper deals with the results obtained from the experiments on rotatory dispersion of TAA.