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• W2040921187 startingPage "363" @default.
• W2040921187 abstract "The tumor-associated cell surface antigens (TAA) gp 71 and AgI cocap H-2, but are not associated with H-2 following solubilization of membrane with detergent. We have attempted to solubilize intact TAA/H-2 complexes from surface-labeled L cells using decreasing concentrations of the nonionic detergent Nonidet-P 40 (NP 40). Associations between gp 71 and H-2 and between AgI and H-2 in solution were detected using sequential immunoprecipitation. gp 71/H-2 and AgI/H-2 complexes were solubilized at the lowest detergent concentration used, 0.01% NP 40. No coprecipitation of these antigen pairs was seen at any higher NP 40 concentration tested. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed lthat precipitation of antigens solulbilized in 0.01% NP 40 leads to coprecipitation of a small number of other protein peaks and does not appear to involve wholesale inclusion of labeled membrane proteins. These results, together with previous observations of cocapping between TAA and H-2 antigens, suggest that the molecules are associated with one another in the membrane. Detergent solubilization of membranes with all but the most gentle conditions leads to disruption of these complexes." @default.
• W2040921187 created "2016-06-24" @default.
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• W2040921187 date "1980-05-01" @default.
• W2040921187 modified "2023-09-25" @default.
• W2040921187 title "Solubilization of complexes between tumor-associated and H-2 antigens from a tumor cell plasma membrane" @default.
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• W2040921187 doi "https://doi.org/10.1002/eji.1830100509" @default.
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