作者: Dinah S. Seidl , Werner G. Jaffé , Eglis González , Antonio Calleias
DOI: 10.1016/0003-2697(78)90439-6
关键词: Casein 、 Biochemistry 、 Electrophoresis 、 Substrate (chemistry) 、 Chromatography 、 Digestion 、 Amido Black 、 Trypsin 、 Subtilisin 、 Filter paper 、 Biology 、 Biophysics 、 Cell biology 、 Molecular biology
摘要: Abstract A microelectrophoretic method for the detection of proteinase inhibitors is deseribed. Microscope slides covered with agar gel containing casein were used electrophoretic separation proteins from bean seeds. Subsequently, a filter paper strip saturated solution known concentration. After 60 min digestion, strips removed, and stained amido black. Blue spots appeared where substrate was protected digestion by presence inhibitors. Single seed or leaf extracts can be studied this method. Different trypsin inhibition patterns observed samples different varieties. An inhibitor subtilisin detected in all Ph. vulgaris studied.