Purification and properties of an alpha-amylase inhibitor from wheat.
Four inhibitors of alpha-amylase (EC 3.2.1.1) were separated from an alcohol extract of wheat by ion-exchange chromatography on DE52-cellulose. One inhibitor, which showed the greatest specificity for human salivary amylase relative to human pancreatic amylase, has been purified by the following steps: (a) alcohol fractionation (60--90%) of water extract (b) ion-exchange chromatography on QAE-Sephadex A-50; (c) re-chromatography on DE52-cellulose and (d) gel filtration on Sephadex G-50. The purified inhibitor is 100 times more specific for human salivary amylase than for human pancreatic amylase. It shows an electrophoretic mobility of 0.2 on disc gel electrophoresis and a molecular weight of about 21 000. This inhibitor contributes about 16% to the total salivary amylase inhibiting power of the wheat extract.
D000681:Amylases / Q000037:antagonists & inhibitors*; D004791:Enzyme Inhibitors / Q000302:isolation & purification*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010179:Pancreas / Q000201:enzymology; D010944:Plants / Q000378:metabolism*; D012463:Saliva / Q000201:enzymology; D014908:Triticum
D004791:Enzyme Inhibitors; D000681:Amylases