ALTERATIONS IN ERYTHROCYTE BAND 3 ORGANIZATION INDUCED BY THE PHOTOSENSITIZER, HEMATOPORPHYRIN DERIVATIVE

Abstract
Photosensitization of erythrocytes in the presence of hematoporphyrin derivative causes cross-linking of membrane proteins. This cross-linking is associated with partial lysis of the cells and an increased susceptibility to heat-induced membrane fragmentation. The effect of photosensitization on the organization of erythrocyte band 3 was monitored using the technique of time-resolved phosphorescence anisotropy. Band 3 rotational diffusion was somewhat restricted upon photooxidation, indicating aggregation of this major integral membrane protein.