| Autor: |
Lasoh, Jürgen, Iwig, Marting, Hanson, Horst |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 1972, Vol. 27 Issue 3, p431-435, 5p |
| Abstrakt: |
Leucine aminopeptidase from bovine eye lenses was taken as a model enzyme for the elaboration of a simple and sensitive visualization method of matrix-bound proteins, which is widely applicable and does not rely on special catalytic properties of the insolubilized proteins. To this end the fluorochrome fluorescein isothiocyanate was covalently attached to either the enzyme prior to coupling to Sephadex G-100 or Sepharose 6B with the BrCN method or to the corresponding antibody. The fluorescein-labelled enzyme retained a good deal of its biological function as judged from its catalytic activity and immunological reactivity. After coupling the fluorescein-labelled enzyme to the support beads, fluoromicrographs of the whole spheres and of 10-μm thick bead sections (swollen state) were taken in order to study and visualize the enzyme distribution across the gel structure. In addition, an alternative way of spotting the carrier-bound enzyme utilizing the immunological precipitation reaction with fluorescein-tagged antibody to the enzyme has been tried. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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