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Stopped-flow fluorescence and steady-state kinetic studies of ligand-binding reactions of glucoamylase from Aspergillus niger

✍ Scribed by Karsten OLSEN; Birte SVENSSON; Ulla CHRISTENSEN


Book ID
115129649
Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
745 KB
Volume
209
Category
Article
ISSN
1432-1327

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Binding of isomaltose and maltose to the
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The binding of maltose, isomaltose, and D-glucono-1,5-lactone to the glucoamylase [E.C.3.2.1.3] from Aspergillus niger was monitored by the fluorescence-intensity change (delta F) based on the tryptophan residues of the enzyme, and the binding parameters (Kd and delta Fmax) were evaluated from the d