Abstract
Polyethylene glycol (PEG) was substituted for ammonium sulfate in the gradient solubilization chromatographic procedure for the purification of proteins. Preliminary studies utilizing this method for fractionation of a crude lysyl hydroxylase preparation yielded an increase both in purity and in recovery of activity when compared with fractional precipitation with PEG. Turbidity, evident in resuspended fractional precipitates, was not found in PEG gradient solubilization fractions containing enzymatic activity.