Purification and Characterization of a Novel Sialidase from a Strain of Arthrobacter nicotianae

[subscript m] = 49°C and 48°C), determined by CD spectroscopy. The isoenzymes are less stable against denaturation with Gdn.HCl, and the free energy of stabilization in water was calculated to be 7.6 and 8.0 kJ mol⁻¹, respectively. The specific activity (K [subscript m] value) toward glucomacropepti...

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Veröffentlicht in:	Journal of biochemistry (Tokyo) 2005-03, Vol.137 (3), p.365-371
Hauptverfasser:	Abrashev, Ignat, Dulguerova, Gabriela, Dolashka-Angelova, Pavlina, Voelter, Wolfgang
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Arthrobacter - enzymology Arthrobacter nicotianae circular dichroism Electrophoresis, Polyacrylamide Gel Enzyme Stability Fluorescence Hydrogen-Ion Concentration Isoenzymes - chemistry Isoenzymes - isolation & purification Isoenzymes - metabolism Kinetics Molecular Sequence Data Neuraminidase - chemistry Neuraminidase - isolation & purification Neuraminidase - metabolism neuraminidases PAGE polyacrylamide gel electrophoresis Protein Conformation Protein Denaturation protein sequencing quantum yield sialidase EC 32.1.18 substrate specificity Temperature TFA Thermodynamics trifluoroacetic acid Tryptophan - chemistry ultraviolet absorption
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Zusammenfassung:	[subscript m] = 49°C and 48°C), determined by CD spectroscopy. The isoenzymes are less stable against denaturation with Gdn.HCl, and the free energy of stabilization in water was calculated to be 7.6 and 8.0 kJ mol⁻¹, respectively. The specific activity (K [subscript m] value) toward glucomacropeptide as a substrate was calculated to be 0.126 mM for NA1 and 0.083 mM for NA2.
ISSN:	0021-924X 1756-2651
DOI:	10.1093/jb/mvi053