Assay for protease inhibitors: qualitative measurement and detection in polyacrylamide gel electrophoretograms.
A simple and fast method for qualitative measurement of protease inhibitors has been developed. The high sensitivity of the assay is based on a casein-precipitating reaction at pH 5.5. Cellulose paper strips, moistened with protease inhibitor-containing solutions, are applied to the surface of an agar-skim milk gel previously coated with a protease solution. After incubation for 2 h at 37 degrees C, inhibitory activity is indicated by a translucent zone (absence of casein degradation) on a white background of precipitated small casein fragments. In addition to being useful for rapid screening of a large number of complex samples, the method allows the localization of protease inhibitor activity in sodium dodecyl sulfate-polyacrylamide gel electrophoretograms.
Grenier
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Département de Santé Buccale, Faculté de Médecine Dentaire, Université de Montréal, Canada.
D000362:Agar; D000818:Animals; D002364:Caseins / Q000378:metabolism; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D008892:Milk; D011480:Protease Inhibitors / Q000032:analysis*; D014357:Trypsin / Q000378:metabolism; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000032:analysis
D002364:Caseins; D011480:Protease Inhibitors; D000362:Agar; D014360:Trypsin Inhibitor, Kunitz Soybean; D002918:Chymotrypsin; D014357:Trypsin