Low molecular organic inactivators in differentiating organ origin of alpha-amylase in humans. Part I

Alpha-amylases derived from pancreatic juice, saliva and granulocytes show different sensitivity to the low molecular organic inactivators. Pancreatic alpha-amylase is more susceptible to inhibitory activity of d-glyceraldehyde and d-mannitol and glycerol in comparison to alpha-amylase from saliva and granulocytes. Iodoacetate and urea exhibited inhibitory activity against granulocytic alpha-amylase and only a minute inactivation of salivary and pancreatic alpha-amylases was found. The most effective inhibition against all tested alpha-amylases was noted with dihydroxyacetone. We should stress, no evident differences were noted in the degree of sensitivity to this inactivator of the tested enzymes. The presumable mechanism of the inactivation of alpha-amylases with low molecular organic inactivators is briefly discussed. The procedure for the differentiation of organ origin of alpha-amylases is suggested.