Protein chromatography on adsorbents with hydrophobic and ionic groups. Purification of human erythrocyte glycophorin
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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.
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1990 ◽
Vol 7
(2)
◽
pp. 255-259
◽
2008 ◽
Vol 139
(1-3)
◽
pp. 104-109
◽
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