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Literature DB >> 3954734

A bovine epithelial membrane protein that binds polymeric immunoglobulin and has a structure related to that of bovine secretory component.

Abstract

A protein of Mr 94000 was isolated from detergent-solubilized bovine intestinal, liver and mammary-gland membranes. It binds immunoglobulin M and also undergoes proteolytic fragmentation in a similar manner to bovine secretory component (Mr 74000). The affinity-purified membrane protein is therefore most likely to be the bovine epithelial receptor for polymeric immunoglobulin. A structural model is proposed.

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Year: 1986 PMID： 3954734 PMCID： PMC1152982 DOI： 10.1042/bj2330037

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

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References

19 in total

1. Studies on translocation of immunoglobulins across intestinal epithelium. IV. Evidence for binding of IgA and IgM to secretory component in intestinal epithelium.

Authors: W R Brown; K Isobe; P K Nakane; B Pacini
Journal: Gastroenterology Date: 1977-12 Impact factor: 22.682

6. Mucosal and glandular distribution of immunoglobulin components: differential localization of free and bound SC in secretory epithelial cells.

Authors: P Brandtzaeg
Journal: J Immunol Date: 1974-04 Impact factor: 5.422

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

Authors: D Beale
Journal: Biochem J Date: 1985-08-01 Impact factor: 3.857

8. Silver stain for detecting 10-femtogram quantities of protein after polyacrylamide gel electrophoresis.

Authors: K Ohsawa; N Ebata
Journal: Anal Biochem Date: 1983-12 Impact factor: 3.365

9. Bovine secretory component. Isolation, molecular size and shape, composition, and NH2-terminal amino acid sequence.

Authors: R S Labib; N J Calvanico; T B Tomasi
Journal: J Biol Chem Date: 1976-04-10 Impact factor: 5.157

10. Fragmentation and reduction of bovine secretory component. Preparation of a biologically active fragment and some evidence for a multiple-domain structure.

Authors: D Beale; J G Hopley
Journal: Biochem J Date: 1985-03-15 Impact factor: 3.857

A bovine epithelial membrane protein that binds polymeric immunoglobulin and has a structure related to that of bovine secretory component.

1. Studies on translocation of immunoglobulins across intestinal epithelium. IV. Evidence for binding of IgA and IgM to secretory component in intestinal epithelium.

2. Intestinal epithelial cell surface membrane glycoprotein synthesis. I. An indicator of cellular differentiation.

3. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

4. Isolation of human secretory component by affinity chromatography on IgM-sepharose.

5. The receptor for transepithelial transport of IgA and IgM contains multiple immunoglobulin-like domains.

6. Mucosal and glandular distribution of immunoglobulin components: differential localization of free and bound SC in secretory epithelial cells.

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

8. Silver stain for detecting 10-femtogram quantities of protein after polyacrylamide gel electrophoresis.

9. Bovine secretory component. Isolation, molecular size and shape, composition, and NH2-terminal amino acid sequence.

10. Fragmentation and reduction of bovine secretory component. Preparation of a biologically active fragment and some evidence for a multiple-domain structure.