Characterization of high pI α-glucosidase from germinated barley seeds: substrate specificity, subsite affinities and active-site residues

This publication has 35 references indexed in Scilit:

• Effects of Bay m 1099, an α-Glucosidase Inhibitor, on Starch Metabolism in Germinating Wheat Seeds
  Bioscience, Biotechnology, and Biochemistry, 1994
• A quantitative assessment of the importance of barley seed α-amylase, β-amylase, debranching enzyme, and α-glucosidase in starch degradation
  Archives of Biochemistry and Biophysics, 1991
• Degradation of Native Starch Granules by Barley α-Glucosidases
  Plant Physiology, 1990
• Carbon Metabolism in Alfalfa Root Nodules: Developmental Patterns of Host Plant Enzymes Before and After Shoot Removal¹
  Crop Science, 1984
• Specific Determination of α-Amylase Activity in Crude Plant Extracts Containing β-Amylase
  Plant Physiology, 1983
• Subsite structure and ligand binding mechanism of glucoamylase
  Molecular and Cellular Biochemistry, 1983
• [41] Cathepsin B, cathepsin H, and cathepsin L
  Published by Elsevier ,1981
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• 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