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Precipitation of Soluble Affinity Complexes by a Second Affinity Interaction: A Model Study
Author(s) -
Senstad C.,
Mattiasson B.
Publication year - 1989
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1989.tb00050.x
Subject(s) - concanavalin a , lactate dehydrogenase , dextran , chemistry , precipitation , affinity chromatography , lectin , dehydrogenase , biochemistry , chromatography , enzyme , in vitro , physics , meteorology
Lactate dehydrogenase was purified by affinity precipitation. The enzyme bound to Blue Dextran (the Cibacron blue residues) and was precipitated by addition of concanavalin A. The lectin functions as a crosslinking agent, building up large flocs of dextran that subsequently precipitate, thus co‐precipitating the affinity‐bound lactate dehydrogenase.