The kinetic characteristics of galactose-l-phosphate uridyl transferase have been determined in homogenates of human liver biopsies obtained from control subjects and in 50-fold purified enzyme preparations from liver obtained at autopsy. A standardized assay procedure employing linear kinetics was used to assess the enzyme activity in homogenates of liver biopsy specimens from five control subjects and four patients with congential galactosemia with demonstrated absence of the enzyme activity in red blood cells. Activity of control specimens ranged from 11.8 to 17.2 mμmoles of UDPgalactose formed per min mg of protein. Liver of two galactosemic patients, both Caucasian, possessed no detectable enzyme activity (less than 1-2% of normal). The tissue of two others, both Negro, who are known to be capable of metabolizing intravenously administered galactose, contained easily detectable enzyme at approximately 10% of the controls. No alternate enzymatic activity for formation of UDPgalactose was found in the liver of Negroes with galactosemia that was as active as the residual galactose-l-phosphate uridyl transferase. The data suggest that the residual liver enzyme activity accounts for the ability of Negroes with galactosemia to metabolize limited but significantly large quantities of galactose.