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Characterisation of monoclonal antibodies which specifically recognise the human erythrocyte glucose transport protein.
Author(s) -
Boyle J.M.,
Whetton A.D.,
Dexter T.M.,
Meeran K.,
Baldwin S.A.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb04050.x
Subject(s) - monoclonal antibody , biology , antibody , biochemistry , microbiology and biotechnology , genetics
Two monoclonal antibodies (mabs) of subclass IgG1 have been raised against the human erythrocyte glucose transport protein. The mabs bound to the purified glucose transporter in both its membrane‐bound and detergent‐solubilised forms. However, they exhibited little or no binding to the detergent‐solubilised nucleoside transport protein, which is present as a minor contaminant in the glucose transport protein preparation. Both mabs inhibited the binding of cytochalasin B to the glucose transport protein, reducing the affinity of this binding by greater than 2‐fold. Each mab labelled the transporter polypeptide on Western blots both before and after treatment of the protein with endoglycosidase F, indicating that the epitopes recognised were located on the protein moiety of the glycoprotein. However, the mabs did not bind to the large fragments produced by tryptic or chymotryptic digestion of the native protein, although both mabs were shown to bind to sites on the cytoplasmic surface of the erythrocyte membrane.