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• W2022611929 startingPage "438" @default.
• W2022611929 abstract "The enzymatic iodination technique has been utilized in a study of the externally disposed membrane proteins of the mouse L cell. Iodination of cells in suspension results in lactoperoxidase-specific iodide incorporation with no loss of cell viability under the conditions employed, less than 3% lipid labeling, and more than 90% of the labeled species identifiable as monoiodotyrosine. 90% of the incorporated label is localized to the cell surface by electron microscope autoradiography, with 5-10% in the centrosphere region and postulated to represent pinocytic vesicles. Sodium dodecylsulfate-polyacrylamide gels of solubilized L-cell proteins reveals five to six labeled peaks ranging from 50,000 to 200,000 daltons. Increased resolution by use of gradient slab gels reveals 15-20 radioactive bands. Over 60% of the label resides in approximately nine polypeptides of 80,000 to 150,000 daltons. Various controls indicate that the labeling pattern reflects endogenous membrane proteins, not serum components. The incorporated 125-I, cholesterol, and one plasma membrane enzyme marker, alkaline phosphodiesterase I, are purified in parallel when plasma membranes are isolated from intact, iodinated L cells. The labeled components present in a plasma membrane-rich fraction from iodinated cells are identical to those of the total cell, with a 10- to 20-fold enrichment in specific activity of each radioactive peak in the membrane." @default.
• W2022611929 created "2016-06-24" @default.
• W2022611929 creator A5021509115 @default.
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• W2022611929 date "1975-02-01" @default.
• W2022611929 modified "2023-10-16" @default.
• W2022611929 title "Externally disposed plasma membrane proteins. I. Enzymatic iodination of mouse L cells." @default.
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• W2022611929 doi "https://doi.org/10.1083/jcb.64.2.438" @default.
• W2022611929 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2109506" @default.
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