Affinity column purification of amylases on protein inhibitors from wheat kernel.
An affinity column was devised for the purification of a large number of amylases inhibited by the albumin from wheat kernel. The procedure involved linking the protein inhibitors from wheat to Sepharose and then specifically eluting the amylase adsorbed to the gel with a high concentration of maltose. By this procedure, the amylases from Tenebrio molitor L. (yellow mealworm) larvae and chicken pancreas were purified to homogeneity with good yields for the first time, as shown by both alkaline and acidic electrophoresis. Human saliva alpha-amylase, purified by the same procedure, showed specific activity and electrophoretic patterns similar to those obtained by other workers with different techniques.
D000327:Adsorption; D000681:Amylases / Q000302:isolation & purification*; D000818:Animals; D002645:Chickens; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors; D005782:Gels; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010179:Pancreas / Q000201:enzymology; D010940:Plant Proteins / Q000032:analysis*; D012463:Saliva / Q000201:enzymology; D014908:Triticum / Q000032:analysis
D004791:Enzyme Inhibitors; D005782:Gels; D010940:Plant Proteins; D000681:Amylases