Abstract
The contribution of secretory component to the stability of secretory IgA against proteolysis has been studied by a new approach, i.e., by comparing the proteolytic degradation of IgA dimers with the degradation of the complexes formed in vitro between these proteins and secretory component. The results show that attachment of secretory component to the dimeric backbone of the secretory IgA molecule is accompanied by a significantly increased resistance of this backbone against digestion by both trypsin and pepsin. This protective effect may be a physiologic function of secretory component or may be due merely to unspecific blocking by secretory component of one or more sensitive peptide bonds in the IgA backbone.
Footnotes
-
↵1 This investigation was supported by Research Grant 13X-4212 to I. Björk from the Swedish Medical Research Council and by a grant from the Medical Faculty of the University of Uppsala.
- Received June 24, 1974.
- Copyright © 1975 by The American Association of Immunologists, Inc.
Pay Per Article - You may access this article (from the computer you are currently using) for 1 day for US$37.50
Regain Access - You can regain access to a recent Pay per Article purchase if your access period has not yet expired.