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

Mannitol dehydrogenase (D-mannitol:NADP+ 2-oxidoreductase, (C 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 onl...

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Veröffentlicht in:	Carbohydrate research 1991, Vol.216, p.505-509
Hauptverfasser:	Berezenko, S, Sturgeon, R.J
Format:	Artikel
Sprache:	eng
Schlagworte:	Agaricus bisporus Analytical, structural and metabolic biochemistry Biological and medical sciences Carbohydrates enzyme activity Fundamental and applied biological sciences. Psychology inhibition mannitol Miscellaneous Other biological molecules oxidoreductases purification
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Zusammenfassung:	Mannitol dehydrogenase (D-mannitol:NADP+ 2-oxidoreductase, (C 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.
ISSN:	0008-6215 1873-426X