The  -amylase of the beetle Callosobruchus chinensis. Purification and action pattern.
Callosobruchus chinensis larval amylase was isolated and purified in five steps, which included co-precipitation with glycogen and column chromatography on ECTEOLA-cellulose. The enzyme was homogeneous by disc gel electrophoresis on polyacrylamide. The alpha-amylase nature was evidenced by the action on amylopectin beta-amylase limit-dextrin, by the effect on the substrate-iodine complex and by the action pattern on several polysaccharide substrates. These action patterns are compared with those of other alpha-amylases.
D000179:Acrylates; D000681:Amylases / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D002482:Cellulose; D011232:Chemical Precipitation; D002845:Chromatography; D001517:Coleoptera / Q000201:enzymology*; D004589:Electrophoresis, Disc; D005782:Gels; D006003:Glycogen / Q000378:metabolism; D007455:Iodine / Q000378:metabolism; D007814:Larva / Q000201:enzymology; D011134:Polysaccharides / Q000378:metabolism
D000179:Acrylates; D005782:Gels; D011134:Polysaccharides; D002482:Cellulose; D006003:Glycogen; D007455:Iodine; D000681:Amylases