Resonance Raman Spectra of Methylorange Bound to Proteins and Cationic Surfactants

Resonance Raman spectra of methylorange were recorded for aqueous solutions containing various proteins and cationic surfactants. The base form of methylorange was found to retain its trans-azo structure on the interaction with human serum albumin and with cetyltrimethylammonium bromide. The relative intensities of the Raman bands at 1420 cm−1 and at 1155 cm−1 of methylorange change appreciably along with the shift of the absorption maximum in the visible and ultraviolet region on addition of proteins and surfactants.