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Stopped-flow kinetic studies on the binding of gluconolactone and maltose to glucoamylase

โœ Scribed by Tanaka, Akiyoshi; Ohnishi, Masatake; Hiromi, Keitaro

Book ID
126154672
Publisher
American Chemical Society
Year
1982
Tongue
English
Weight
760 KB
Volume
21
Category
Article
ISSN
0006-2960

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Binding of isomaltose and maltose to the
Binding of isomaltose and maltose to the glucoamylase from Aspergillus niger, as studied by fluorescence spectrophotometry and steady-state kinetics
โœ Masatake Ohnishi; Takashi Matsumoto; Tatsuya Yamanaka; Keitaro Hiromi ๐Ÿ“‚ Article ๐Ÿ“… 1990 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 676 KB

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