Protein chromatography on adsorbents with hydrophobic and ionic groups. Purification of human erythrocyte glycophorin.

ABSTRACT: 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.

SUBMITTER: Simmonds RJ 

PROVIDER: S-EPMC1164711 | biostudies-other | 1977 May

REPOSITORIES: biostudies-other