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pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat
Rat and rabbit IgG immunoglobulins conjugated to horseradiah peroxidase as a histochemical marker bind at 0 degrees C to the luminal surface of absorptive cells in isolated segments of jejunum from 10-12-day old rats. Binding is observed at pH 6.0, near the normal luminal pH of the duodenum and jeju...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1976
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109747/ https://www.ncbi.nlm.nih.gov/pubmed/11223 |
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collection | PubMed |
description | Rat and rabbit IgG immunoglobulins conjugated to horseradiah peroxidase as a histochemical marker bind at 0 degrees C to the luminal surface of absorptive cells in isolated segments of jejunum from 10-12-day old rats. Binding is observed at pH 6.0, near the normal luminal pH of the duodenum and jejunum at this age, but not at pH 7.4. Furthermore, no binding occurs when cells are exposed at pH 6.0 to either free peroxidase or peroxidase conjugated to chicken or sheep IgG immunoglobulins or bovine serum albumin. The sensitivity of binding to pH suggests a means whereby immunoglobulins which are selectively absorbed by the cells can be released efficiently at the abluminal surface. |
format | Text |
id | pubmed-2109747 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1976 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21097472008-05-01 pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat J Cell Biol Articles Rat and rabbit IgG immunoglobulins conjugated to horseradiah peroxidase as a histochemical marker bind at 0 degrees C to the luminal surface of absorptive cells in isolated segments of jejunum from 10-12-day old rats. Binding is observed at pH 6.0, near the normal luminal pH of the duodenum and jejunum at this age, but not at pH 7.4. Furthermore, no binding occurs when cells are exposed at pH 6.0 to either free peroxidase or peroxidase conjugated to chicken or sheep IgG immunoglobulins or bovine serum albumin. The sensitivity of binding to pH suggests a means whereby immunoglobulins which are selectively absorbed by the cells can be released efficiently at the abluminal surface. The Rockefeller University Press 1976-11-01 /pmc/articles/PMC2109747/ /pubmed/11223 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat |
title | pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat |
title_full | pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat |
title_fullStr | pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat |
title_full_unstemmed | pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat |
title_short | pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat |
title_sort | ph-dependent binding of immunoglobulins to intestinal cells of the neonatal rat |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109747/ https://www.ncbi.nlm.nih.gov/pubmed/11223 |