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Erythrocyte band 3 protein strongly interacts with phosphoinositides
Author(s) -
Hanicak Andreas,
Maretzki Dieter,
Reimann Barbara,
Pap Eward,
Visser Antonie J.W.G.,
Wirtz Karel W.A.,
Schubert Dieter
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00595-8
Subject(s) - phosphatidylinositol , chemistry , biochemistry , tryptophan , band 3 , phosphatidylinositol 4,5 bisphosphate , pyrene , membrane protein , biophysics , membrane , phosphorylation , biology , amino acid , organic chemistry
85% of the phosphorus coisolated with band 3 protein during separation of the intrinsic proteins of the human erythrocyte membrane by zonal electrophoresis in high concentrations of acetic acid was found to be derived from phosphoinositides, mainly phosphatidylinositol 4,5‐bisphosphate. When native band 3 protein and pyrene‐labelled phospholipids were present in micelles of the nonionic detergent nonaethyleneglycol lauryl ether, strong resonance energy transfer was observed between the tryptophan residues and phosphatidylinositol 4,5‐bisphosphate and, to a smaller degree, phosphatidylinositol 4‐phosphate. We conclude that band 3 protein strongly interacts with phosphoinositides, in particular with phosphatidylinositol 4,5‐bisphosphate.