Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Carbohydrate Sequence
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Chromatography, Ion Exchange
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Electrophoresis, Polyacrylamide Gel
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Fungal Proteins / isolation & purification*
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Fungal Proteins / metabolism
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Galactose / metabolism
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Mannose / metabolism
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Membranes, Artificial
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Molecular Sequence Data
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Oligosaccharides / metabolism
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Penicillium / enzymology*
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Polyvinyls
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Sequence Homology, Amino Acid
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Substrate Specificity
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alpha-Galactosidase / isolation & purification*
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alpha-Galactosidase / metabolism*
Substances
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Fungal Proteins
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Membranes, Artificial
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Oligosaccharides
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Polyvinyls
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polyvinylidene fluoride
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alpha-Galactosidase
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Mannose
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Galactose