Abstract
An examination of the ultraviolet spectra
of methyl orange and related dyes in various solvents has indicated that the
spectral changes occurring on adding proteins to an aqueous solution of methyl
orange are not the result of strong electrostatic interactions (PNH3+
. . . -02SR) as suggested by earlier workers. It is
proposed that the interaction of methyl orange with protein generally produces
two types of spectral effect : (i) an absorptivity increase and bathochromic
shift resulting from electronic interaction of dimethylamino, azo, and/or
sulphonate groups in the dye with the protein, and (ii) an absorptivity
decrease and hypsochromic shift resulting from out-of-plane twisting of the
dye's conjugated system by the establishment of the above electronic
interactions. In most cases the second effect predominates, giving the
absorptivity decrease and hypsochromic shift usually observed.
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16 articles.
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