Immunichemical determination of cathodal elastase in human duodenal juice.
In human duodenal juice enzymes hydrolysing the elastase substrate succinyl-trialanine-p-nitroanilide have both an anodal and cathodal mobility in agarose gel electrophoresis. The cathodal enzyme, also having an elastinolytic activity, was purified. An application of electroimmunoassay for separate determination of this cathodal elastase is presented. Parallel estimations of esterolytic, elastinolytic and immunochemical activities in duodenal juice from a group of children revealed discrepancies suggesting both variations in the distribution of the two forms of "elastases", and presence of inactive forms.
D000328:Adult; D000813:Anilides / Q000378:metabolism; D002648:Child; D002675:Child, Preschool; D002850:Chromatography, Gel; D003429:Cross Reactions; D004386:Duodenum; D006801:Humans; D007106:Immune Sera; D005779:Immunodiffusion; D007123:Immunoelectrophoresis, Two-Dimensional; D007223:Infant; D007419:Intestinal Secretions / Q000201:enzymology*; D009842:Oligopeptides / Q000378:metabolism; D010196:Pancreatic Elastase / Q000032:analysis*
D000813:Anilides; D007106:Immune Sera; D009842:Oligopeptides; C015516:succinyl-trialanine-4-nitroanilide; D010196:Pancreatic Elastase