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Thiol‐fatty acylation of the glucose transport protein of human erythrocytes
Author(s) -
James M. May
Publication year - 1990
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(90)81344-n
Subject(s) - hydroxylamine , immunoprecipitation , chemistry , biochemistry , thiol , acylation , monoclonal antibody , glucose transporter , incubation , antibody , biology , gene , insulin , endocrinology , catalysis , immunology
Incubation of intact human erythrocytes with [ 3 H]palmitate labeled a protein with electrophoretic characteristics of the glucose transporter. This labeling occurred via a thioester linkage, since it was unaffected by organic solvent extraction, but was substantially removed as the hydroxamate upon treatment with neutral hydroxylamine. Immunoprecipitation of the labeled protein with a monoclonal antibody to the glucose transporter confirmed its identity.