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Lysozyme optical rotation

Fig. 18. Temperature-dependence of absorbance and optical rotation of lysozyme, pH 2.2, 0.10 M KCl (after Foss, 1961 redrawn by Foss, 1962). Fig. 18. Temperature-dependence of absorbance and optical rotation of lysozyme, pH 2.2, 0.10 M KCl (after Foss, 1961 redrawn by Foss, 1962).
A new technique for the rapid measurement of ultrasonic absorption with a sampling interval of 5 msec has been developed and applied to a kinetic study of denaturation and subsequent reduction of hen egg-white lysozyme. The rate constant of denaturation by guanidinium chloride obtained from the time variance of ultrasonic absorption agreed well with that from u.v. absorption and optical rotation. Analysis of the constants as functions of reagent concentrations indicated that the intermediate state between native and reduced state is not necessarily the completely denatured state. [Pg.463]


See other pages where Lysozyme optical rotation is mentioned: [Pg.148]    [Pg.325]    [Pg.367]    [Pg.367]    [Pg.68]    [Pg.496]    [Pg.497]    [Pg.527]    [Pg.202]    [Pg.351]    [Pg.375]    [Pg.36]    [Pg.34]    [Pg.290]   
See also in sourсe #XX -- [ Pg.488 ]




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