Biochemical characterization of chicken secretory component
- 1 January 1986
- journal article
- research article
- Published by Wiley in European Journal of Immunology
- Vol. 16 (3) , 225-229
- https://doi.org/10.1002/eji.1830160303
Abstract
Human dimeric IgA was injected i.v. into chickens whose bile was then collected. The human IgA which had been transported across the hepatocytes of the chicken was subsequently purified from the bile and shown to be associated with a protein of 80 kDa and pI 4.6, which reacted with rabbit antisera to chicken bile proteins but not with an antiserum to human α chain. The chicken bile protein thus has functional and biochemical properties similar to those of mammalian secretory component.This publication has 20 references indexed in Scilit:
- The receptor for transepithelial transport of IgA and IgM contains multiple immunoglobulin-like domainsNature, 1984
- COMPARATIVE ASPECTS OF THE HEPATOBILIARY TRANSPORT OF IgA*Annals of the New York Academy of Sciences, 1983
- A functional homologue of mammalian secretory component exists in chickensEuropean Journal of Immunology, 1982
- The sacrificial receptor-translocation of polymeric IgA across epitheliaTrends in Biochemical Sciences, 1982
- The origin of IgA in chicken bile: its rapid active transport from bloodEuropean Journal of Immunology, 1981
- Isolation and characterization of secretory IgA (sIgA) and free secretory component (FSC) from rat bileMolecular Immunology, 1980
- Endocytic vesicles in liver carry polymeric IgA from serum to bileBiochimica et Biophysica Acta (BBA) - General Subjects, 1979
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Human Secretory ComponentScandinavian Journal of Immunology, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970