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Jakobovits, A., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Eshdat, Y., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Sharon, N., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
A new approach is described for the isolation of lectin receptors without the use of detergents, by plucking them from the cell surface. Cells bound to lectin-coated Sepharose beads are sheared off the beads by mechanical disruption, whereupon the receptors remain attached to the beads and are released specifically by inhibitory sugars. Material plucked from neuraminidase-treated human erythrocytes by beads coated with peanut agglutinin and released by D-galactose was identified as asialoglycophorin. The same membrane glycoprotein was plucked from neuraminidase-treated erythrocytes by beads coated with soybean agglutinin, but at considerably lower yield. © 1981.
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Plucking of lectin receptors from erythrocytes: Isolation of cell surface components without the use of detergents
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Jakobovits, A., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Eshdat, Y., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Sharon, N., Department of Biophysics, The Weizmann Institute of Science, Rehovoth, Israel
Plucking of lectin receptors from erythrocytes: Isolation of cell surface components without the use of detergents
A new approach is described for the isolation of lectin receptors without the use of detergents, by plucking them from the cell surface. Cells bound to lectin-coated Sepharose beads are sheared off the beads by mechanical disruption, whereupon the receptors remain attached to the beads and are released specifically by inhibitory sugars. Material plucked from neuraminidase-treated human erythrocytes by beads coated with peanut agglutinin and released by D-galactose was identified as asialoglycophorin. The same membrane glycoprotein was plucked from neuraminidase-treated erythrocytes by beads coated with soybean agglutinin, but at considerably lower yield. © 1981.
Scientific Publication
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