Antibody raised against the purified human erythrocyte glucose transporter specifically precipitated four proteins from normal and Rous sarcoma virus-transformed chicken embryo cells: a major protein of Mr 41,000 and minor proteins of Mr 68,000, 73,000, and 82,000. The Mr 41,000 and 82,000 proteins were found only in a membrane fraction, not in the soluble fraction, and displayed a heterogeneous mobility on NaDodSO4/polyacrylamide gel electrophoresis, suggesting glycosylation. The Mr 41,000 and 82,000 proteins were increased in amount after malignant transformation in direct proportion to the increase in hexose transport rate, and the increase was dependent on the expression of the src gene product, as revealed with a temperature-conditional src mutant. We suggest that the Mr 41,000 and 82,000 proteins are the glucose transporter of chicken embryo fibroblasts, or a component of the glucose transporter. These experiments provide direct evidence that malignant transformation increases the rate of glucose transport by increasing the number of transporters in the membrane.