Purification and some properties of alpha-galactosidase from Penicillium purpurogenum.
alpha-Galactosidase was purified by ion-exchange chromatographies on DEAE-cellulose and SE-cellulose columns from the culture filtrate of Penicillium purpurogenum No. 618. The final preparation was judged homogeneous by SDS-PAGE and its molecular mass and isoelectric point were estimated to be 67 kDa and 4.1, respectively. The N-terminal amino acid sequence of the enzyme was analyzed and aligned with those of other alpha-galactosidases. In addition, the enzyme acted on the stubbed alpha-galactosyl residue connected to the beta-1,4-manno-oligosaccharide chain, indicating that this specificity was quite different from that of Mortierella vinacea alpha-galactosidase.
Shibuya
H
H
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Kobayashi
H
H
Park
G G
GG
Komatsu
Y
Y
Sato
T
T
Kaneko
R
R
Nagasaki
H
H
Yoshida
S
S
Kasamo
K
K
Kusakabe
I
I
D000595:Amino Acid Sequence; D002240:Carbohydrate Sequence; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D005690:Galactose / Q000378:metabolism; D008358:Mannose / Q000378:metabolism; D008567:Membranes, Artificial; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000378:metabolism; D010407:Penicillium / Q000201:enzymology*; D011145:Polyvinyls; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D000519:alpha-Galactosidase / Q000302:isolation & purification* / Q000378:metabolism*; D005465:Fluorocarbon Polymers
D005656:Fungal Proteins; D005690:Galactose; D008358:Mannose; D008567:Membranes, Artificial; D009844:Oligosaccharides; D011145:Polyvinyls; D000519:alpha-Galactosidase; C024865:polyvinylidene fluoride; D005465:Fluorocarbon Polymers