Sepharose-bound erythropoientin. Studies with anti-erythropoietin.
A T Ichiki, Yvonne P. Quirin, Ruth N. Shelton, R. D. Lange
Abstract
A T Ichiki, Yvonne P. Quirin, Ruth N. Shelton, R. D. Lange
Abstract
Anti-erythropoietin antibodies (anti-ESF) were determined by the capacity of the immunoglobulins to neutralize the biological activity of erythropoietin (ESF). Affinity chromatographic methods were used to initiate the purification of anti-ESF by use of ESF covalently linked to Sepharose. It was observed that anti-ESF bound the ESF-Sepharose. In order to remove the nonspecific immunoglobulins, the anti-ESF preparation was subjected to further chromatography on affinity colums where either serum or urinary proteins from a polycythemic patient were covalently linked to Sepharose. It was demonstrated the affinity chromatography could be used as a method isolate anti-ESF.
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Anti-erythropoietin antibodies (anti-ESF) were determined by the capacity of the immunoglobulins to neutralize the biological activity of erythropoietin (ESF). Affinity chromatographic methods were used to initiate the purification of anti-ESF by use of ESF covalently linked to Sepharose. It was observed that anti-ESF bound the ESF-Sepharose. In order to remove the nonspecific immunoglobulins, the anti-ESF preparation was subjected to further chromatography on affinity colums where either serum or urinary proteins from a polycythemic patient were covalently linked to Sepharose. It was demonstrated the affinity chromatography could be used as a method isolate anti-ESF.
Key concepts: Sepharose, Affinity chromatography, Antibody, Chemistry, Erythropoietin, Chromatography, Covalent bond, Specific activity