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ALTERATIONS IN ERYTHROCYTE BAND 3 ORGANIZATION INDUCED BY THE PHOTOSENSITIZER, HEMATOPORPHYRIN DERIVATIVE
Author(s) -
Beaton S.,
McPherson R. A.,
Tilley L.
Publication year - 1995
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1995.tb05281.x
Subject(s) - hematoporphyrin , photosensitizer , lysis , chemistry , biophysics , membrane , fragmentation (computing) , photochemistry , biochemistry , photodynamic therapy , biology , organic chemistry , ecology
— 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.