I mTRODVCTIONThe absorption of light by rhodopsin in the retina activates the pigment molecules and leads eventually to the stimulation of rod vision. The initial light reaction is followed by a sequence of thermal reactions occurring equally in light or darkness, by which the rhodopsin, a conjugated carotenoid protein, ultimately bleaches to retinenel and protein (Wald, Durell, and St. George, 1950). The work described here deals with the initial activation of rhodopsin.Rhodopsin can be bleached not only by light but by heat. At 50°C. or above it bleaches rapidly in the dark and at a rate that is very temperature-dependent. Lythgoe and Quilliam (1938) calculated an experimental activation energy of 44 kg. cal. per mole from their data on the temperature coefficient in neutral solutions. On the other hand, the rate of bleaching by white light is not temperature-dependent, showing that no thermal activation is needed (Hecht, 1920-21).The purpose of the following research was to study the transition between photic and thermal activation. The argument runs as follows. On going from shorter wave lengths to red light a point should be reached beyond which the incident quanta cannot supply the entire energy needed to activate the rhodopsin molecule. If bleaching is to occur nonetheless, the deficit will have to be met by a contribution of thermal energy from the internal degrees of freedom of the molecule. There should therefore be a critical wave length beyond which the bleaching by light becomes temperature-dependent.Measurement of the temperature coefficient of bleaching at intervals along the wave length scale showed that a temperature dependence does in fact appear in the orange at about 590 mu. Moreover, the quantum energy at this wave length differs very little from the activation energy observed in heat bleaching. At wave lengths longer than 590 mt~, the temperature coefficient increases regularly so that the sum of the energy of the absorbed quanta and the thermal ac-