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Updated: Aug 18, 2026

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
09:37

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

Published on: August 15, 2014

The immunoglobulin structure of human anti-M agglutinins

M L Smith, M L Beck

    Transfusion
    |July 1, 1979
    PubMed

    Fifty examples of human anti-M agglutinins were subjected to reductive cleavage using both 2-mercaptoethanol (2-ME) and dithiothreitol (DTT). Thirty-nine (78%) were resistant to inactivation by sulphydryl compounds indicating IgG composition. This was confirmed by column chromatography. The remaining eleven sera were sensitive to reduction cleavage. There was no obvious association of immunoglobulin composition of the antibody with previous immune exposure to the M antigen. These results confirm observations in the literature that anti-M agglutinins are an exception to the generally expected correlation of saline agglutinating activity with IgM structure.

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