Immunoelectron microscopic double labeling of alkaline phosphatase and penicillinase with colloidal gold in frozen thin sections of Bacillus licheniformis 749/C
| Autor: | Tinglu Guan, B. K. Ghosh, Arati Ghosh |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Phosphatase
Bacillus Microbiology Frozen Sections Bacillus licheniformis Colloids Binding site Molecular Biology chemistry.chemical_classification Chromatography biology Histocytochemistry Penicillinase biology.organism_classification Alkaline Phosphatase Microscopy Electron Membrane Enzyme chemistry Biochemistry Cytoplasm Colloidal gold Immunoglobulin G Alkaline phosphatase Gold Research Article |
| Zdroj: | Journal of bacteriology. 164(1) |
| ISSN: | 0021-9193 |
| Popis: | The subcellular distribution of alkaline phosphatase and penicillinase was determined by double labeling frozen thin sections of Bacillus licheniformis 749/C with colloidal gold-immunoglobulin G (IgG). Antipenicillinase and anti-alkaline phosphatase antibodies were used to prepare complexes with 5- and 15-nm colloidal gold particles, respectively. The character of the labeling of membrane-bound alkaline phosphatase and penicillinase was different: the immunolabels for alkaline phosphatase (15-nm particles) were bound to a few sites at the inner surface of the plasma membrane, and the gold particles formed clusters of various sizes at the binding sites; the immunolabels for penicillinase (5-nm particles), on the other hand, were bound to the plasma membrane in a dispersed and random fashion. In the cytoplasm, immunolabels for both proteins were distributed randomly, and the character of their binding was similar. The labeling was specific: pretreating the frozen thin sections with different concentrations of anti-alkaline phosphatase or penicillinase blocked the binding of the immunolabel prepared with the same antibody. Binding could be fully blocked by pretreatment with 800 micrograms of either antibody per ml. |
| Databáze: | OpenAIRE |
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