Glucose transport carrier of human erythrocytes. Radiation-target size of glucose-sensitive cytochalasin B binding protein.

Apparent molecular sizes of D-glucose-sensitive cytochalasin B binding protein of human erythrocyte membranes are assessed by applying classical target theory to irradiation-inactivation data. Molecular weights of this protein as it occurs in untreated ghosts, EDTA-treated ghosts, and reconstituted vesicles of Triton extract of ghosts are 220,000, 180,000, and 220,000, respectively. These results, in conjunction with other findings in the literature, suggest that the native form of the glucose transport carrier of human erythrocytes is a tetrameric assembly of a 50,000-dalton monomer or is a dimer of 100,000 daltons.