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

Pamela Stanley, J. P. Carver

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)617-622
Number of pages6
JournalJournal of Cell Biology
Volume79
Issue number3
StatePublished - 1978

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Wheat Germ Agglutinins
Agglutination
Cricetulus
Ovary
Membranes
Glutaral
Binding Sites
Temperature

ASJC Scopus subject areas

  • Cell Biology

Cite this

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title = "Binding of [125I]wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components",
abstract = "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.",
author = "Pamela Stanley and Carver, {J. P.}",
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volume = "79",
pages = "617--622",
journal = "Journal of Cell Biology",
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T1 - Binding of [125I]wheat germ agglutinin to Chinese hamster ovary cells under conditions which affect the mobility of membrane components

AU - Stanley, Pamela

AU - Carver, J. P.

PY - 1978

Y1 - 1978

N2 - 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.

AB - 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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SP - 617

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