Identification of the Membrane Attachment Sites for Protein 4.1 in the Human Erythrocyte (∗)

• Published in: The Journal of biological chemistry Vol. 270; no. 10; pp. 5360 - 5366
• Main Authors: Hemming, Nicola J., Anstee, David J., Staricoff, Marcelo A., Tanner, Michael J.A., Mohandas, Narla
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 10.03.1995; American Society for Biochemistry and Molecular Biology
• Subjects: Binding Sites; Chymotrypsin; Cytoskeletal Proteins; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Erythrocyte Membrane - metabolism; Glycophorins - chemistry; Glycophorins - isolation & purification; Glycophorins - metabolism; Humans; Kinetics; Membrane Proteins - chemistry; Membrane Proteins - isolation & purification; Membrane Proteins - metabolism; Models, Structural; Neuropeptides; Protein Conformation; Trypsin

The nature of the membrane attachment site(s) for protein 4.1 in the human erythrocyte membrane has yet to be fully elucidated. In this paper we show that the major attachment site is glycophorin (GP) C/D, and that purified protein 4.1 can bind to two distinct sites on glycophorin C/D. One of these...