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Binding of [125I] wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components

The binding of [125I]wheat germ agglutinin ([125I]WGA) of high specific activity to Chinese hamster ovary (CHO) cells has been examined over a millionfold range of WGA concentrations and correlated with the phenomena of agglutination and capping by WGA. Analysis of the binding data by the method of...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1978
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110266/
https://www.ncbi.nlm.nih.gov/pubmed/103881
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collection PubMed
description The binding of [125I]wheat germ agglutinin ([125I]WGA) of high specific activity to Chinese hamster ovary (CHO) cells has been examined over a millionfold range of WGA concentrations and correlated with the phenomena of agglutination and capping by WGA. Analysis of the binding data by the method of Scatchard gives a complex curve indicative of positive cooperativity amongst high-affinity binding sites. Binding assays performed under conditions which inhibit capping and/or agglutination, such as low temperature or glutaraldehyde fixation, give similarly complex binding curves. Thus, the gross mobility of WGA receptors in the membrane does not appear to be responsible for the cooperative binding of WGA to CHO cells.
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spelling pubmed-21102662008-05-01 Binding of [125I] wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components J Cell Biol Articles The binding of [125I]wheat germ agglutinin ([125I]WGA) of high specific activity to Chinese hamster ovary (CHO) cells has been examined over a millionfold range of WGA concentrations and correlated with the phenomena of agglutination and capping by WGA. Analysis of the binding data by the method of Scatchard gives a complex curve indicative of positive cooperativity amongst high-affinity binding sites. Binding assays performed under conditions which inhibit capping and/or agglutination, such as low temperature or glutaraldehyde fixation, give similarly complex binding curves. Thus, the gross mobility of WGA receptors in the membrane does not appear to be responsible for the cooperative binding of WGA to CHO cells. The Rockefeller University Press 1978-12-01 /pmc/articles/PMC2110266/ /pubmed/103881 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
Binding of [125I] wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components
title Binding of [125I] wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components
title_full Binding of [125I] wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components
title_fullStr Binding of [125I] wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components
title_full_unstemmed Binding of [125I] wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components
title_short Binding of [125I] wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components
title_sort binding of [125i] wheat germ agglutinin to chinese hamster ovary cells under conditions which affect the mobility of membrane components
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110266/
https://www.ncbi.nlm.nih.gov/pubmed/103881