Tryptic digestion of bovine secretory IgA at elevated temperature and in urea. Isolation of SC domain 1 which is covalently bound to IgA dimer and binds non-covalently to IgM-Reference-Cited by-同舟云学术

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Tryptic digestion of bovine secretory IgA at elevated temperature and in urea. Isolation of SC domain 1 which is covalently bound to IgA dimer and binds non-covalently to IgM

Published:1989-01 Issue:5 Volume:21 Page:549-554
ISSN:0020-711X
Container-title:International Journal of Biochemistry
language:en
Short-container-title:International Journal of Biochemistry

Author:

Beale D.

Publisher

Elsevier BV

Subject

Biochemistry

Reference21 articles.

1. Differences in fragmentation between bound and unbound bovine secretory component suggest a model for its interaction with polymeric immunoglobulin;Beale;Biochem. J.,1985

2. The structure of bovine secretory component;Beale;Vet. Immun. Immunopath.,1987

3. Cyanogen bromide cleavage of bovine secretory component and its tryptic fragments;Beale;Int. J. Biochem.,1988

4. The sites of tryptic cleavage in bovine secretory component. Structural and functional implications;Beale;Biochim. biophys. Acta,1987

5. A comparison of the fragmentation of different species of mammalian immunoglobulin M by trypsin in urea;Beale;Comp. Biochem. Physiol.,1983

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Epithelial and Hepatobiliary Transport of Polymeric Immunoglobulins;Handbook of Mucosal Immunology;1994

2. Selective Transport of IgA;Gastroenterology Clinics of North America;1991-09

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