Patterns of action of glucoamylase isozymes from Aspergillus species on glycogen.
Glucoamylase isozymes from black Aspergillus species have been freed of all traces of alpha-amylase by chromatography on Bio-Gel P-100, as evidenced by limited hydrolysis of oxidized amylose. Glucoamylase I retains its ability to hydrolyze rabbit-liver glycogen rapidly. By contrast, glucoamylase II hydrolyzes glycogen slowly, and addition of alpha-amylase to glucoamylase II does not enhance its activity toward glycogen. These results indicate that alpha-amylase is not involved in hydrolysis of glycogen by glucoamylase.
D000681:Amylases; D000818:Animals; D001230:Aspergillus / Q000201:enzymology*; D001234:Aspergillus niger / Q000201:enzymology; D002384:Catalysis; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D004355:Drug Stability; D004588:Electrophoresis, Cellulose Acetate; D004589:Electrophoresis, Disc; D005959:Glucosidases / Q000302:isolation & purification; D006003:Glycogen; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification; D010944:Plants / Q000201:enzymology; D011817:Rabbits; D012233:Rhizopus / Q000201:enzymology
D007527:Isoenzymes; D006003:Glycogen; D000681:Amylases; D005959:Glucosidases