title: Use of charged tails in protein-purification fusions. Polyaspartic acid tails in Aspergillus glucoamylase expressed in yeast.
authors: Department of Biochemistry, University of Turku, Finland.
authors: I
authors: I
authors: Suominen
authors: H
authors: H
authors: Nurmela
authors: H
authors: H
authors: Heimo
authors: C
authors: C
authors: Ford
authors: D
authors: D
authors: Stachon
authors: C
authors: C
authors: Glatz
mesh_terms: D000595:Amino Acid Sequence; D001224:Aspartic Acid; D001230:Aspergillus / Q000201:enzymology; D001483:Base Sequence; D011232:Chemical Precipitation; D003001:Cloning, Molecular; D005656:Fungal Proteins / Q000302:isolation & purification; D005087:Glucan 1,4-alpha-Glucosidase / Q000302:isolation & purification*; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D010957:Plasmids; D015202:Protein Engineering / Q000379:methods*; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae
chemical_list: D005656:Fungal Proteins; D011993:Recombinant Fusion Proteins; D001224:Aspartic Acid; D005087:Glucan 1,4-alpha-Glucosidase