Abstract
Abstract The nature of the intersubunit bonds in rabbit secretory IgA dimer was investigated by employing gel filtration on 2% and 4% agarose columns equilibrated with 6 M guanidine-HCl. Under these conditions, rabbit secretory IgA behaved as a dimer [(H2L2)2] which established that the bonds linking the monomer subunits were covalent in nature. Rabbit secretory component, however, dissociated from the native molecule in 6 M guanidine-HCl, which indicated that the secretory component was bound to the native dimer by non-covalent bonds. Mild reduction and alkylation with dithiothreitol (DTT) in aqueous buffer resulted in dissociation of the rabbit secretory IgA dimer molecule to monomer subunits and lower molecular weight material. Reduction with varying quantities of DTT showed that rabbit secretory IgA dimer was more resistant to reduction than human secretory IgA dimer which in turn was more resistant to reduction than a human IgA dimer myeloma protein.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
