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Preparation of pure albumin and transferrin from rabbit serum using concanavalin sepharose


Zeitschrift fuer Versuchstierkunde 18(5-6): 307-313
Preparation of pure albumin and transferrin from rabbit serum using concanavalin sepharose
Prepurified albumin (ammonium sulfate precipitation, Sephadex G-200 gel chromatography) is bound to Con A [concanavalin A] Sepharose only in small amounts and can be prepared in an almost pure state by Con A-Sepharose chromatography. Accompanying impurities, consisting of .alpha.-globulins, can be removed by preparative electrophoresis. The main amounts of rabbit transferrin are fixed to Con A-Sepharose in an easily reversible manner in contrast to human transferrin. This behavior gives the possibility of enriching transferrin rather selectively using affinity chromatography on Con A-Sepharose. Impurities from albumin can be separated by preparative electrophoresis. The proteins obtained are sufficient for production of monospecific immunosera.

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Accession: 006173740



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Preparation of pure albumin and transferrin from rabbit serum using con A-sepharose. Zeitschrift für Versuchstierkunde 18(5-6): 307-313, 1976

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