Abstract
The preparation of chick serum albumin is described. The preparation was homogeneous at pH 8.53 and 4.50 in the Tiselius electrophoresis apparatus. However, an immunological method showed the presence of three additional minor components. An antiserum, prepared by injection of chick serum albumin into rabbits, was used to demonstrate the net synthesis of serum albumin by chick-liver slices. The results of Peters and Anfinsen (J. Biol. Chem. 186, 805, 1950) were thus confirmed. The incorporation of radioactivity into serum albumin and a soluble protein fraction was studied after incubation of chick-liver slices with (C14) glucose and (C14) alanine respectively. The specific radioactivity of the alanine in each protein fraction was determined. The incorporation of radioactivity into a soluble protein fraction of rat hepatoma and rat liver was studied after incubation of the tissue slices with (14C) glucose. The specific radio-activity of the glucose during the incubation period was followed. It was thus shown that under these conditions there is a better utilization of glucose by hepatoma tissue for the synthesis of protein than there is by liver tissue.