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. 1985 Aug 1;229(3):759–763. doi: 10.1042/bj2290759

Differences in fragmentation between bound and unbound bovine secretory component suggest a model for its interaction with polymeric immunoglobulin.

D Beale
PMCID: PMC1145121  PMID: 4052023

Abstract

Unbound bovine secretory component was cleaved into two-domain and one-domain fragments by trypsin within 1 h. Bovine secretory component covalently bound to bovine IgA dimer, as in secretory IgA, was much more resistant to fragmentation, which did not proceed beyond the three-domain stage even after 5 h. Bovine secretory component non-covalently bound to bovine IgM or to human IgM or IgA polymer was also relatively resistant to fragmentation, which again was largely arrested at the three-domain stage. A model for the binding of secretory component to polymeric immunoglobulin is proposed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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