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Labeling of human erythrocyte membrane proteins by photoactivatable radioiodinated phosphatidylcholine and phosphatidylserine A search for the aminophospholipid translocase
Author(s) -
Zachowski Alain,
Fellmann Pierre,
Hervé Paulette,
Devaux Philippe F.
Publication year - 1987
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(87)80311-3
Subject(s) - translocase , phosphatidylserine , phosphatidylcholine , chemistry , phosphatidylethanolamine , biochemistry , red blood cell , membrane protein , biophysics , membrane , chromosomal translocation , phospholipid , biology , gene
We have synthesized radioiodinated photoactivatable phosphatidylcholine ( 125 ‐N 3 ‐PC) and phosphatidylserine ( 125 I‐N 3 ‐PS). After incubation with red blood cells in the dark, the labeled PC could be extracted but not the corresponding PS molecule, indicating that the latter was transported by the aminophospholipid translocase, but not the former. When irradiated immediately after incorporation, N 3 ‐PS, but not N 3 ‐PC, partially blocked subsequent translocation of spin‐labeled aminophospholipids. Analysis of probe distribution by SDSpolyacrylamide gel electrophoresis revealed that 125 I‐N 3 ‐PS labeled seven membrane bound components with molecular masses between 140 and 27 kDa: one (or several) of these components should correspond to the aminophospholipid translocase.