title: Purification of antifreeze proteins by adsorption to ice.
abstract: Antifreeze proteins (AFPs) can protect organisms from freezing injury by adsorbing to ice and inhibiting its growth. We describe here a method where ice, grown on a cold finger, is used to selectively adsorb and purify these ice-binding proteins from a crude mixture. Type III recombinant AFP was enriched approximately 50-fold after one round of partitioning into ice and purified to homogeneity by a second round. This method can also be used to purify non-ice-binding proteins by linkage to AFP domains as demonstrated by the recovery of a 50 kDa maltose-binding protein-AFP fusion from a crude lysate of Escherichia coli.
authors.affiliation: Department of Biology, Queen's University, Kingston, Ont., Canada K7L 3N6.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Kuiper
authors.forename: Christopher
authors.initials: C
authors.lastname: Lankin
authors.forename: Sherry Y
authors.initials: SY
authors.lastname: Gauthier
authors.forename: Virginia K
authors.initials: VK
authors.lastname: Walker
authors.forename: Peter L
authors.initials: PL
authors.lastname: Davies
mesh_terms: D000327:Adsorption; D000818:Animals; D021343:Antifreeze Proteins, Type III / Q000737:chemistry* / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D005615:Freezing; D007053:Ice / Q000032:analysis; D012034:Refrigeration / Q000295:instrumentation / Q000379:methods
chemical_list: D021343:Antifreeze Proteins, Type III; D007053:Ice