Isolation and properties of glucose-1-phosphatase from mycelia of Pholiota nameko

An acid phosphatase with a very high substrate specificity for glucose-1-phosphate was isolated for the first time from mycelia of Pholiota nameko. The molecular weight of the enzyme was estimated to be 31,000 on gel filtration and 35,000 on SDS-PAGE. The activity was inhibited by Cu2+, Hg2+, molybd...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1998-11, Vol.62 (11), p.2251-2253
Hauptverfasser:	Joh, T. (Niigata Univ. (Japan). Faculty of Agriculture), Yazaki, J, Suzuki, K, Hayakawa, T
Format:	Artikel
Sprache:	eng
Schlagworte:	ACID PHOSPHATASE ACIDE AMINE AMINO ACIDS AMINOACIDOS Analytical, structural and metabolic biochemistry Basidiomycota - enzymology Basidiomycota - ultrastructure Biological and medical sciences Chromatography, Gel ELECTROFORESIS ELECTROPHORESE ELECTROPHORESIS Electrophoresis, Polyacrylamide Gel ENZYME INHIBITORS Enzymes and enzyme inhibitors Escherichia coli Proteins FOSFATASA ACIDA Fundamental and applied biological sciences. Psychology glucose-1-phosphatase Hydrolases INHIBIDORES DE ENZIMAS INHIBITEUR D'ENZYME ISOENZIMAS ISOENZYME ISOENZYMES MICELIO Molecular Weight mushroom MYCELIUM PHOLIOTA Pholiota nameko PHOSPHATASE ACIDE Phosphoric Monoester Hydrolases - isolation & purification PURIFICACION PURIFICATION Substrate Specificity
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Zusammenfassung:	An acid phosphatase with a very high substrate specificity for glucose-1-phosphate was isolated for the first time from mycelia of Pholiota nameko. The molecular weight of the enzyme was estimated to be 31,000 on gel filtration and 35,000 on SDS-PAGE. The activity was inhibited by Cu2+, Hg2+, molybdate, and tartaric acid. The sequence of N-terminal 20 amino acid residues was analyzed
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.62.2251