Abstract
SummaryThe optical rotatory dispersion of solutions of alcohol dehydrogenase (AD), glyceralde‐hyde‐3‐phosphate dehydrogenase (GAPD), glutamic dehydrogenase (GAD), and malic dehydrogenase (MD) was investigated. The b, values of the native dehydrogenases were found to be between ‐170 and ‐450. GAD and MD were studied also with the short wave length ultraviolet light, and they both displayed strong Cotton effects at 230–245 mµ. The solutions of native GAD were found to be dextrorotatory, however, they became levorotatory on denaturation with alkali, urea, or sodium decyl sulfate. According to the rotatory dispersion data, the dehydrogenases belong to the α‐helical globular proteins, although it seems premature to make quantitative estimates of the a‐helix content from the rotatory dispersion data alone.
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