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A BALB/c mouse IgA myeloma protein that binds salmonella flagellar protein
Journal of Immunology (Baltimore, Md. : 1950)
|June 1, 1975
Abstract:
A BALB/c IgA mouse myeloma protein in ascites (MOPC-467) had been found to bind an antigen in heat extracts from Salmonella, Pasteurella, and Herellea cultures. MOPC-467 ascites was shown to immobilize motile S. adelaide, agglutinate formalin fixed S. MILWAUKEE, AND PURIFIED IgA (M467) was capable of precipitating column-purified flagella and flagellin from S. milwaukee.
Insights
A mouse myeloma protein, MOPC-467 IgA, binds bacterial antigens. This immunoglobulin effectively immobilizes and agglutinates specific bacterial strains, demonstrating its antigen-binding capabilities.
Area of Science:
- Immunology
- Microbiology
Background:
- BALB/c IgA mouse myeloma protein (MOPC-467) exhibits antigen-binding properties.
- Previous studies indicated MOPC-467 binds antigens from Salmonella, Pasteurella, and Herellea.
Purpose of the Study:
- To characterize the functional activity of MOPC-467 IgA against bacterial components.
- To investigate the specific interactions between MOPC-467 and bacterial antigens.
Main Methods:
- Utilized MOPC-467 ascites for bacterial immobilization and agglutination assays.
- Employed purified IgA (M467) for precipitation of flagella and flagellin from S. milwaukee.
Main Results:
- MOPC-467 ascites demonstrated the ability to immobilize motile S. adelaide.
- Formalin-fixed S. MILWAUKEE were agglutinated by MOPC-467 ascites.
- Purified IgA (M467) successfully precipitated flagella and flagellin from S. milwaukee.
Conclusions:
- MOPC-467 IgA possesses specific binding and functional activity against bacterial antigens.
- The study confirms the utility of MOPC-467 in targeting bacterial components like flagella.