Protein chromatography on adsorbents with hydrophobic and ionic groups. Purification of human erythrocyte glycophorin.
Human erythrocyte glycophorin was purified rapidly by (a) chromatography of a Triton X-100 extract of erythrocyte 'ghosts' on N-(3-carboxypropionyl)aminodecyl-Sepharose in buffers containing Triton X-100 or sodium dodecyl sulphate, or (b) chromatography of whole 'ghosts', solubilized in sodium dodecyl sulphate, on dodecyl-Sepharose, in buffers containing sodium dodecyl sulphate. The products contained 85-95% glycophorin (electrophoretic band PAS-1) and the major contaminants were glycoproteins PAS-2 (possibly a subunit of glycophorin) and PAS-3.
D002850:Chromatography, Gel; D004910:Erythrocyte Membrane / Q000032:analysis; D004912:Erythrocytes / Q000032:analysis; D006021:Glycophorins / Q000302:isolation & purification*; D006801:Humans; D012685:Sepharose; D012795:Sialoglycoproteins / Q000302:isolation & purification*
D006021:Glycophorins; D012795:Sialoglycoproteins; D012685:Sepharose