The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Isolation and characterization of an Fc receptor from neonatal rat small intestine
Abstract
Receptors for the Fc region of IgG from neonatal rat intestinal brush borders were solubilized using 3‐[(3‐cholamidopropyl)dimethyl‐ammonio]‐l‐propane sulfonate and purified by affinity chromatography. Analysis of IgG‐binding material by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis under reducing conditions reveals two components with apparent M r of 41 000‐50 000 and 15 000. The larger component is glycosylated and may dimerize, giving a 100‐110‐kDa band on nonreduced gels. Both proteins are localized in the proximal small intestine, where IgG is specifically taken up during the first three weeks of neonatal life, and disappear when specific transport stops after weaning. Electron irradiation of brush borders shows that the functional unit for IgG binding has a molecular weight in sifu of 110 kDa. These data suggest that a dimer of the 41‐50‐kDa protein together with the 15 kDa and other proteins may mediate intestinal transport of maternal IgG.
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Cites
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Cited by
FcRn: the neonatal Fc receptor comes of age
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IgG placental transfer in healthy and pathological pregnancies
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An Fc receptor structurally related to MHC class I antigens
Simister, N. E., & Mostov, K. E. (1989) · Nature · doi:10.1038/337184a0 · Cited by 729
Self-citationEngineering the Fc region of immunoglobulin G to modulate in vivo antibody levels
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Metadata
- Authors
- Simister, N. E., & Rees, A. R.
- Venue
- European Journal of Immunology
- Publisher
- Wiley
- Published
- 1985-01
- Volume
- 15
- Issue
- 7
- Pages
- 733-738
- ISSN
- 0014-2980 (ISSN-L)
- 1521-4141
- OpenAlex
- W2111462418
- Cited by
- 339
- References
- 17
- FWCI
- 1.64
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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