Abstract:
:IgM was purified from normal human colostrum and salivary secretions devoid of IgA. The isolated immunoglobulin was found to contain J chain, and showed a slight affinity for free secretory component (SC). In the secretions IgM was saturated with SC, but only 60--70 per cent of the molecules had retained the component after purification. Moreover, the I determinant of SC was much more exposed in secretory IgM than in secretory IgA, indicating a relatively 'loose' quaternary structure of the former immunoglobulin. Paired immunofluorescence staining demonstrated that secretory epithelial cells of colonic glands contained IgM in exactly the same distribution as IgA. IgM appearing in exocrine secretions is therefore a true secretory immunoglobulin in contrast to IgG. However, the quaternary structure of secretory IgM is less covalently stabilized than that of secretory IgA.
journal_name
Immunologyjournal_title
Immunologyauthors
Brandtzaeg Psubject
Has Abstractpub_date
1975-09-01 00:00:00pages
559-70issue
3eissn
0019-2805issn
1365-2567journal_volume
29pub_type
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