Abstract
1. The properties of rhodopsin in solution have been examined in preparations from marine fishes, frogs, and mammals. 2. The bleaching of neutral rhodopsin in solution includes a photic and at least three thermal ("dark") processes. Thermal reactions account for approximately half the total fall in extinction at 500 mµ. 3. Bleaching has been investigated at various pH's from 3.9 to about 11. With increase in pH the velocity of the thermal components increases rapidly. Though the spectrum of rhodopsin itself is scarcely affected by change in pH, the spectra of all product-mixtures following irradiation are highly pH-labile. 4. The spectrum of pure rhodopsin—or of the rhodopsin chromophore—is fixed within narrow limits. The extinction at 400 mµ lies between 0.20 to 0.32 of that at the maximum. 5. Within the limitations of available data, the spectrum of pure rhodopsin corresponds in form and position with the spectral sensitivity of human rod vision, computed at the retinal surface. 6. The nature of bleaching of rhodopsin in solution, its kinetics, and its significance in the retinal cycle are discussed.

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