The enzymic determination of D-mannitol with mannitol dehydrogenase from Agaricus bisporus

S. Berezenko; R. J. Sturgeon

doi:10.1016/0008-6215(92)84185-U

The enzymic determination of D-mannitol with mannitol dehydrogenase from Agaricus bisporus

S. Berezenko, R. J. Sturgeon

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11 Citations (Scopus)

Abstract

Mannitol dehydrogenase (D-mannitol:NADP⁺ 2-oxidoreductase, EC 1.1.1.138), isolated from the sporocarps of Agaricus bisporus, has been purified 120-fold following fractionation with protamine sulphate, followed by hydrophobic and affinity chromatography. D-Mannitol and D-fructose appear to be the only substrate and products involved in the reaction, having K_m values of 7.5 and 9.8mM, respectively. The purified enzyme has been used for the determination of D-mannitol and also the D-mannose content of glycoproteins and polysaccharides following the liberation of that hexose and reduction to D-mannitol.

Original language	English
Pages (from-to)	505-509
Number of pages	5
Journal	Carbohydrate Research
Volume	216
DOIs	https://doi.org/10.1016/0008-6215(92)84185-U
Publication status	Published - 2 Sept 1991

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title = "The enzymic determination of D-mannitol with mannitol dehydrogenase from Agaricus bisporus",

abstract = "Mannitol dehydrogenase (D-mannitol:NADP+ 2-oxidoreductase, EC 1.1.1.138), isolated from the sporocarps of Agaricus bisporus, has been purified 120-fold following fractionation with protamine sulphate, followed by hydrophobic and affinity chromatography. D-Mannitol and D-fructose appear to be the only substrate and products involved in the reaction, having Km values of 7.5 and 9.8mM, respectively. The purified enzyme has been used for the determination of D-mannitol and also the D-mannose content of glycoproteins and polysaccharides following the liberation of that hexose and reduction to D-mannitol.",

author = "S. Berezenko and Sturgeon, \{R. J.\}",

year = "1991",

month = sep,

day = "2",

doi = "10.1016/0008-6215(92)84185-U",

language = "English",

volume = "216",

pages = "505--509",

journal = "Carbohydrate Research",

issn = "0008-6215",

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T1 - The enzymic determination of D-mannitol with mannitol dehydrogenase from Agaricus bisporus

AU - Berezenko, S.

AU - Sturgeon, R. J.

PY - 1991/9/2

Y1 - 1991/9/2

N2 - Mannitol dehydrogenase (D-mannitol:NADP+ 2-oxidoreductase, EC 1.1.1.138), isolated from the sporocarps of Agaricus bisporus, has been purified 120-fold following fractionation with protamine sulphate, followed by hydrophobic and affinity chromatography. D-Mannitol and D-fructose appear to be the only substrate and products involved in the reaction, having Km values of 7.5 and 9.8mM, respectively. The purified enzyme has been used for the determination of D-mannitol and also the D-mannose content of glycoproteins and polysaccharides following the liberation of that hexose and reduction to D-mannitol.

AB - Mannitol dehydrogenase (D-mannitol:NADP+ 2-oxidoreductase, EC 1.1.1.138), isolated from the sporocarps of Agaricus bisporus, has been purified 120-fold following fractionation with protamine sulphate, followed by hydrophobic and affinity chromatography. D-Mannitol and D-fructose appear to be the only substrate and products involved in the reaction, having Km values of 7.5 and 9.8mM, respectively. The purified enzyme has been used for the determination of D-mannitol and also the D-mannose content of glycoproteins and polysaccharides following the liberation of that hexose and reduction to D-mannitol.

UR - https://www.scopus.com/pages/publications/0026414075

U2 - 10.1016/0008-6215(92)84185-U

DO - 10.1016/0008-6215(92)84185-U

M3 - Article

SN - 0008-6215

VL - 216

SP - 505

EP - 509

JO - Carbohydrate Research

JF - Carbohydrate Research

ER -

The enzymic determination of D-mannitol with mannitol dehydrogenase from Agaricus bisporus

Abstract

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