Sedimentation equilibrium studies on protein from kookaburra beak.
Fractionated samples of the soluble S-carboxymethyl proteins from kookaburra beak (Frenkel and Gillespie 1976) were examined by equilibrium sedimentation. The molecular weight was found to be 11,300 when the photoelectric scanning absorption optical system was employed and 13,700 when Rayleigh interference optics were used. Possible explanations for this difference are considered and it is concluded that it must arise from heterogeneity of the protein. Optical rotatory dispersion measurements indicate that the proteins probably exist as random coils in dilute aqueous buffer.
D000818:Animals; D001502:Beak / Q000032:analysis*; D001717:Birds / Q000378:metabolism*; D007368:Interferometry; D008027:Light; D008970:Molecular Weight; D009905:Optical Rotatory Dispersion; D011506:Proteins / Q000032:analysis*; D014461:Ultracentrifugation
D011506:Proteins