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In addition to the degradation of <jats:sup>125<\/jats:sup>I\u2010labeled Ma\u03bc to trichloroacetic acid (TCA) soluble material, a distinct pattern of larger <jats:sup>125<\/jats:sup>I\u2010Map fragments was detected in all sources of B cells tested. The particular fragmentation pattern, as revealed by sodium dodecyl sulfate\u2010polyacrylamide gel electrophoretic analysis, involved the cleavage of both peptide bonds and disulfide bridges. This type of antibody fragmentation appeared to be a selective mechanism associated with sIgM, as no other degradation than that leading to TCA\u2010soluble material could be detected after the internalization and degradation of radiolabeled monoclonal antibodies towards a variety of non\u2010Ig B cell surface receptors. Three fragments of <jats:sup>125<\/jats:sup>I\u2010Ma\u03bc degradation were also detected in the supernatant of Ramos cells, implying that the recycling and exocytosis of certain <jats:sup>125<\/jats:sup>I\u2010Ma\u03bc fragments also took place.<\/jats:p>","DOI":"10.1002\/eji.1830160314","type":"journal-article","created":{"date-parts":[[2007,2,28]],"date-time":"2007-02-28T23:01:48Z","timestamp":1172703708000},"page":"286-291","source":"Crossref","is-referenced-by-count":12,"title":["Internalization and processing of antibodies to surface antigens on human B cells. 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