title: Determination of enterokinase activity by measuring the disappearance of trypsinogen.
abstract: An electrophoretic technique for the determination of enterokinase activity is described. The natural substrate trypsinogen is hydrolysed in the presence of soybean trypsin inhibitor. Under the conditions of assay, neither the trypsin inhibitor nor the trypsin-trypsin inhibitor complex are detected. Enterokinase activity can be determined in biological materials such as duodenal aspirates without any interference from trypsin activity. A significant correlation exists between the present technique and a spectrophotometric technique by which the liberation of trypsin activity is used to determine enterokinase activity.
authors.affiliation: Department of Pediatrics, University of Leuven, Belgium.
authors.forename: H A
authors.initials: HA
authors.lastname: Carchon
authors.forename: E
authors.initials: E
authors.lastname: Jansen
authors.forename: E
authors.initials: E
authors.lastname: Eggermont
mesh_terms: D000293:Adolescent; D002021:Buffers; D002648:Child; D002675:Child, Preschool; D004586:Electrophoresis / Q000379:methods; D004765:Enteropeptidase / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007223:Infant; D013053:Spectrophotometry; D014361:Trypsin Inhibitors / Q000378:metabolism*; D014362:Trypsinogen / Q000378:metabolism*
chemical_list: D002021:Buffers; D014361:Trypsin Inhibitors; D014362:Trypsinogen; D004765:Enteropeptidase