作者: Jurgen LASCH , Martin IWIG , Horst HANSON
DOI: 10.1111/J.1432-1033.1972.TB01856.X
关键词:
摘要: Leucine aminopeptidase from bovine eye lenses was taken as a model enzyme for the elaboration of simple and sensitive visualization method matrix-bound proteins, which is widely applicable does not rely on special catalytic properties insolubilized proteins. To this end fluorochrome fluorescein isothiocyanate covalently attached to either prior coupling Sephadex G-100 or Sepharose 6B with BrCN corresponding antibody. The fluorescein-labelled retained good deal its biological function judged activity immunological reactivity. After support beads, fluoromicrographs whole spheres 10-μm thick bead sections (swollen state) were in order study visualize distribution across gel structure. In addition, an alternative way spotting carrier-bound utilizing precipitation reaction fluorescein-tagged antibody has been tried.