THE Jonn~n~ OF BIOLOGICAL CHEMISTRY
نویسنده
چکیده
Osmotic pressure technique has been employed to investigate the polymerization of bovine cw,-casein B under different experimental conditions. Results at neutral pH indicate that the polymerization of a,-casein B depends much more on ionic strength than on temperature. The number average molecular weight of a,-casein B in 0.01 M KCI, pH 7, at 20” was found to be 29,400 which corresponds to the monomer, whereas the value at 0.1 M KC1 corresponds to that of a trimer. Viscosity and diffusion data suggest that even though cy.casein B is more flexible and possibly more solvated than a common globular protein, it is much more compact than a denatured protein. The results of the optical rotatory dispersion study indicate that there is no gross conformational change as the protein is polymerized from monomer to trimer or tetramer.
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