Binding of isomaltose and maltose to the glucoamylase from Aspergillus niger, as studied by fluorescence spectrophotometry and steady-state kinetics

This publication has 23 references indexed in Scilit:

• Characterization, by the binding of d-mannonolactone, of the subsites adjacent to the catalytic site of glucoamylase from Rhizopus niveus
  Carbohydrate Research, 1987
• Steady-State and Transient Kinetic Studies on the Binding of Maltooligosaccharides to Glucoamylase
  The Journal of Biochemistry, 1983
• Subsite structure and ligand binding mechanism of glucoamylase
  Molecular and Cellular Biochemistry, 1983
• Stopped-flow kinetic studies on the binding of gluconolactone and maltose to glucoamylase
  Biochemistry, 1982
• Kinetics studies on the interactin of rhizopus glucoamylase with maltodextrin and maltotriose, utilizing the absorbance change near 300 nm
  Carbohydrate Research, 1978
• Studies on the Subsite Structure of Amylases. III. Inhibition by Gluconolactone of the Hydrolysis of Maltodextrin Catalyzed by Glucoamylase1 from Rhizopus niveus2
  The Journal of Biochemistry, 1976
• Studies on the Subsite Structure of Amylases
  The Journal of Biochemistry, 1975
• Transient Kinetics of Gloucoamylase1-catalyzed Hydrolysis of Maltodextrin Studied by the Fluorescence Stopped-flow Method2
  The Journal of Biochemistry, 1974
• Subsite affinities of glucoamylase: Examination of the validity of the subsite theory
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
• Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exo-enzyme
  Biochemical and Biophysical Research Communications, 1970