Application of novel monoclonal antibodies in the purification, quantification, and immunohistological localization of the proteinase inhibitor α2-macroglobulin
| Autor: | C. W. E. Justus, Sabine Müller, Michael D. Kramer |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
medicine.diagnostic_test
medicine.drug_class Bioengineering Biology Monoclonal antibody Immunofluorescence Applied Microbiology and Biotechnology Biochemistry Molecular biology Macroglobulin Affinity chromatography Antigen Immunoassay medicine biology.protein Immunohistochemistry Antibody Biotechnology |
| Zdroj: | Enzyme and Microbial Technology. 10:524-531 |
| ISSN: | 0141-0229 |
| DOI: | 10.1016/0141-0229(88)90044-0 |
| Popis: | Monoclonal antibodies (moAbs) recognizing human α 2 -macroglobulin (hMG), a broad-spectrum proteinase inhibitor present in plasma and the interstitial fluid, were developed and characterized. hMG-specific moAbs were found useful (1) to purify the inhibitor molecule via one-step immunoaffinity chromatography; (2) to identify hMG by immunochemical methods (i.e., immunoblotting) in complex biological samples; (3) to quantify hMG by means of a moAb-based enzyme immunoassay; and (4) to localize the antigen by immunohistological methods. By immunofluorescence studies on normal human skin we localized hMG to the epidermo-dermal junction, indicating that this proteinase inhibitor may play an important role in the physiology of the human integument. Taken together, these antibodies appear as powerful tools for the purification of hMG and for immunochemical and immunohistological studies on this molecule. |
| Databáze: | OpenAIRE |
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