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Does sphingomyelin inhibit the erythrocyte anion transport system?
Author(s) -
Scheuring Uwe,
Haase Winfried,
Schubert Dieter
Publication year - 1988
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(88)80738-5
Subject(s) - band 3 , sphingomyelin , vesicle , chemistry , phosphatidylcholine , erythrocyte membrane , efflux , transport protein , biochemistry , ion transporter , membrane , membrane transport , red blood cell , biophysics , phospholipid , biology
The anion transport protein of the human erythrocyte membrane, band 3, was incorporated into unilamellar sphingomyelin vesicles. The vesicles showed a rapid sulfate efflux which could be inhibited by specific inhibitors of the erythrocyte anion transport system. All band 3 molecules contributing to the inhibitor‐sensitive flux component were arranged ‘right‐side‐out’. The turnover number of the transport protein for sulfate transport was virtually identical to that in phosphatidylcholine bilayers and around 6 times larger than in human erythrocyte membranes. Thus, in contrast to other claims, sphingomyelin does not inhibit the erythrocyte anion transport system.