[Bifunctional inhibitor of alpha-amylase/trypsin from wheat grain].
A trypsin inhibitor, isolated from whole-wheat grain (Triticum aestivum L.) by the method of bio-specific chromatography on trypsin-Sepharose, was potent in inhibiting human salivary alpha-amylase. The bi-functional alpha-amylase/trypsin inhibitor was characterized by a narrow specificity for other alpha-amylases and proteinases. The high thermostability of the inhibitor was lost in the presence of SH group-reducing agents. The inhibitor-trypsin complex retained its activity against alpha-amylase. The inhibitor-alpha-amylase complex was active against trypsin. Studies of the enzyme kinetics demonstrated that the inhibition of alpha-amylase and trypsin was noncompetitive. Our results suggest the existence of two independent active sites responsible for the interaction with the enzymes.
Islamov
R A
RA
Furusov
O V
OV
D006801:Humans; D007700:Kinetics; D012639:Seeds / Q000737:chemistry; D013379:Substrate Specificity; D014908:Triticum / Q000737:chemistry*; D014357:Trypsin / Q000737:chemistry*; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D000516:alpha-Amylases / Q000037:antagonists & inhibitors* / Q000737:chemistry
D014361:Trypsin Inhibitors; D000516:alpha-Amylases; D014357:Trypsin