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Separation of Le a and A Human Plasma Antigens
Author(s) -
Andresen P. H.,
Goldman F.,
Henriksen L.
Publication year - 1968
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1111/j.1537-2995.1968.tb02442.x
Subject(s) - size exclusion chromatography , antigen , sepharose , chromatography , chemistry , dialysis , blood proteins , phosphate buffered saline , potassium phosphate , precipitation , biochemistry , immunology , biology , medicine , enzyme , physics , meteorology
The A and Le a specific soluble blood group activities of human plasma were separated from most other proteins by gel filtration on Sepharose columns and from each other by precipitation on dialysis against 1 mM potassium phosphate buffer, pH 6.5. Both antigens emerged from Sepharose columns in fractions normally containing high molecular weight proteins. The Le a antigen was soluble on dialysis, whereas the A antigen was fully precipitated.