Optical rotation and viscosity of native and denatured proteins. X. Further studies on optical rotatory dispersion

The optical rotatory dispersion of serum albumin, α 1-glycoprotein, metal-binding β-globulin, γ-globulin, Bence-Jones protein, β-lactoglobulin, the α- and β-caseins, trypsinogen, chymotrypsinogen, phosvitin, and arachin was studied by means of the Rudolph photoelectric ultraviolet-range spectropolarimeter. It was found that the one-term Drude equation holds in all instances, and that the dispersion constants of the various proteins differ considerably. The unusually low dispersion constants of native γ-globulins were confirmed with this improved method. The Bence-Jones protein and the γ-globulins were identical in their rotatory dispersion behavior. The dispersion constants of phosvitin depend on the acidity of the solutions in the pH range 4–10.