Zonal centrifugation of crude extracts of rat liver shows the presence of two major components of aspartate transcarbamylase, M.W. 900,000 and 600,000. The sedimentation behavior is unaffected by treatment with RNase and detergents. The activity of the ATCase is stabilized in the presence of bovine serum albumin. Experiments in the presence of dithiothreitol or EDTA show that the heavy components do not result from complex formation with albumin. © 1969.