The ultraviolet (UV) denaturation of flying fish myosin, subfragment-I (S-1), and rod was examined by means of solubility test, CD measurement, 8-anilino-1-naphthalene sulfonate (ANS) intensity, and tryptophan fluorescence intensity measurements. Solubilities decreased in order of myosin>rod>S-1 during UV irradiation. CD curves also showed that the α-helical content of myosin and its fragments decreased rapidly with increase of UV intensity and the duration of irradiation. The fluorescence intensities of UV-irradiated myosin-ANS and S-1-ANS decreased after increasing for 10min, but the rod-ANS decreased without increasing. UV irradiation caused a marked decrease in the tryptophan fluorescence intensity of myosin and rod. The SDS-PAGE patterns revealed that myosin heavy chain polymers were formed during UV irradition.
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Ishizaki et al. (1994) studied this question.
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