[Molecular characteristics of beta-galactosidase secreted by Penicillium canescens].
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.
Nikolaev
I V
IV
Khodova
O M
OM
Timokhina
E A
EA
Aleksenko
A Iu
AIu
Vinetskiĭ
Iu P
IuP
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*
D000596:Amino Acids; D005696:Galactosidases; D001616:beta-Galactosidase
Molekuliarnye kharakteristiki sekretiruemoĭ beta-galaktozidzay Penicillium canescans.