Chromatography of Rat Liver Soluble Proteins and Localization of Enzyme Activities

SUMMARY A method was developed for chromatography of rat liver soluble proteins on diethylaminoethyl cellulose, with a parabolic chloride gradient for elution. Protein, nucleic acid and 16 en- zyme activities were determined in the fractions, and each gave a consistent pattern of distribution in a number of preparations. Some of the enzyme activities, for example, lactic dehydro- genase, isomerase, and aldolase, were not adsorbed by the diethyl- aminoethyl cellulose at pH 8.0 and low ionic strength. Several of the enzymes gave multiple peaks of activity. With two of multiple peak enzymes, glucose 6-phosphate dehydrogenase and glutamic oxaloacetic transaminase, rechromatography of one of the peaks, under the same conditions, gave a single peak at the anticipated position. REFERENCES 1. SOBER, H. A., GUTTER, F. J., WYCOFF, M. M., AND PETERSON, E. A., .Z. Am. Chem. Sac., ‘78, 756 (1956). 2. SOBER