title: Large-scale production and purification of recombinant Galanthus nivalis agglutinin (GNA) expressed in the methylotrophic yeast Pichia pastoris.
abstract: The gene coding for agglutinin from Galanthus nivalis (GNA) was expressed in, and secreted by, the methylotrophic yeast, Pichia pastoris. Transformants of P. pastoris were selected and a process to produce and purify gram quantities of recombinant GNA was developed. GNA was secreted at approximately 80 mg l(-1) at the 200 1 scale and was purified to 95% homogeneity using hydrophobic interaction chromatography. The recombinant protein was similar to the protein synthesised in plant with respect to structure and biological activity.
mesh_terms: D000595:Amino Acid Sequence; D019149:Bioreactors / Q000382:microbiology*; D018929:Cell Culture Techniques / Q000379:methods*; D027801:Galanthus / Q000235:genetics / Q000378:metabolism; D037241:Mannose-Binding Lectins / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D010843:Pichia / Q000254:growth & development* / Q000378:metabolism*; D037121:Plant Lectins / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D037241:Mannose-Binding Lectins; D037121:Plant Lectins; D011994:Recombinant Proteins; C063117:snowdrop lectin