Steady-state kinetic and calorimetric studies on the binding of aspergillus niger glucoamylase with gluconolactone, 1-deoxynojirimycin, and β-cyclodextrin

Bioscience, Biotechnology and Biochemistry

Volumn 60, Issue 12, 1996, Pages 2055-2058

  Tanaka, Akiyoshi ^a  

^a MIE UNIVERSITY   (Japan)

Author keywords

Domain interaction; Domain structure; Glucoamylase; Steady state kinetics; Titration calorimetry

Indexed keywords

1 DEOXYNOJIRIMYCIN; BETA CYCLODEXTRIN; BETA CYCLODEXTRIN DERIVATIVE; BETA GLUCONO 1,5 LACTONE; BETA-GLUCONO-1,5-LACTONE; CYCLODEXTRIN; ENZYME INHIBITOR; GLUCAN 1,4 ALPHA GLUCOSIDASE; GLUCONIC ACID; ISOENZYME;

ARTICLE; ASPERGILLUS NIGER; CALORIMETRY; CHEMISTRY; DRUG ANTAGONISM; ENZYMOLOGY; KINETICS; PROTEIN BINDING; THERMODYNAMICS;

1-DEOXYNOJIRIMYCIN; ASPERGILLUS NIGER; BETA-CYCLODEXTRINS; CALORIMETRY; CYCLODEXTRINS; ENZYME INHIBITORS; GLUCAN 1,4-ALPHA-GLUCOSIDASE; GLUCONATES; ISOENZYMES; KINETICS; PROTEIN BINDING; THERMODYNAMICS;

ASPERGILLUS NIGER; RHIZOPUS;

EID: 0030438842     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60.2055     Document Type: Article

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