The protein inhibitors of amylases and peptidases isolated from cereal grains.
The peptidase and amylase inhibitors were isolated from rye and preliminarily purified to investigate some of their properties. It was shown, that both are of albumin character despite the acetic acid solubility of the former. They are not active against the native cereal grain peptidases or amylases (rye, wheat, triticale) but the latter inhibited the animal (hog pancreas, man salivary) and bacterial (Thermamyl, NOVO) alpha-amylases. In the long-term experiments on various rye genotypes there was shown, that the peptidase inhibitor level was rather differentiated between them, but more stable as concerns particular ones. On the other hand the level differentiation of alpha-amylase inhibitor between the genotypes was rather small, but that of climate much more significant.
D000681:Amylases / Q000037:antagonists & inhibitors*; D000818:Animals; D002523:Edible Grain / Q000032:analysis*; D006801:Humans; D010179:Pancreas / Q000201:enzymology; D011480:Protease Inhibitors / Q000302:isolation & purification*; D012469:Salivary Glands / Q000201:enzymology; D012434:Secale / Q000032:analysis; D013552:Swine
D011480:Protease Inhibitors; D000681:Amylases