Free radicals of lysozyme produced by $Ti-H_2O_2$ system were studied in aqueous solution at room temperature using ESR with a continuous flow-mixing. The spectra, each consisting of a doublet with 5.5 G splitting and a broad resonance covering 80 G splitting are closely similar in shape to that for solid irradiated in vacuum at $77^{circ}K$ and observed at room temperature immediately on warming. The result is assumed to indicate that the secondary protein radical components formed within 0.01 second, dead time of the mixing chamber, and initiated by hydrogen atom abstraction at ${alpha}$-carbon atom of peptide chain in liquid solution at room temperature are identical to those resulting from the initial formation of a mixture of positive holes and negative ions by ionization processes as well as radical fragments by the rupture of chemical bonds in the solid during similar time at the same temperature. A broad resonance is observed with considerable amplitude on the high field side of the doublet, which is quite dissimilar to the spectra of irradiated solid lysozyme. This resonance was tentatively attributed to the polypeptide free radical in which unpaired electrons are localized on side chain.