title: [Molecular characteristics of beta-galactosidase secreted by Penicillium canescens].
abstract: Extracellular beta-galactosidase from P. canescens culture medium was purified by ion-exchange chromatography on DEAE and CM-Sepharose CL-6B and gel filtration. The enzyme active form was shown to be a monomer with a molecular weight of about 120 kDa; the isoelectric point is 6.7 and the sedimentation coefficient is 6.5. In terms of physico-chemical and catalytic properties, the purified enzyme is similar to beta-galactosidases of other fungi of genus Penicillium. The amino acid composition and the NH2-terminal sequence of 24 residues non-homologous to the corresponding sequences of bacterial and yeast beta-galactosidases were determined.
authors.forename: I V
authors.initials: IV
authors.lastname: Nikolaev
authors.forename: O M
authors.initials: OM
authors.lastname: Khodova
authors.forename: E A
authors.initials: EA
authors.lastname: Timokhina
authors.forename: A Iu
authors.initials: AIu
authors.lastname: Aleksenko
authors.forename: Iu P
authors.initials: IuP
authors.lastname: Vinetskiĭ
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005696:Galactosidases / Q000378:metabolism*; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D010407:Penicillium / Q000201:enzymology*; D011487:Protein Conformation; D001616:beta-Galactosidase / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D005696:Galactosidases; D001616:beta-Galactosidase
vernacular_title: Molekuliarnye kharakteristiki sekretiruemoĭ beta-galaktozidzay Penicillium canescans.