New Haven, CT Yale University School of Medicine 2/2/1970
3.25 in. x 4 in.
3.25 in. x 4 in. Lantern Slides Original Magnification: x31,000 This study examined the intracellular secretory pathway for IgG using tritiated leucine to tag the protein backbone and tritiated galactose and glucosamine to tag the glycoprotein chains synthesized in the Golgi. EM autoradiography was used to follow the travels of IgG after synthesis. The results indicated that IgG (the major protein synthesized by these myeloma cells) moved from the RER to the Golgi for sugar addition to IgG and likely reached the cell surface via small smooth surfaced transport vesicles. Previously it had been suggested that IgG moved in soluble form through the cytoplasm and was secreted directly through the plasma membrane. No evidence was obtained for temporary storage in secretory granules.
Jamieson, James D
transmission electron micrograph
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Yale University School of Medicine, Department of Cell Biology
George E. Palade Electron Microscopy Slide Collection
See Zagury, D., J.W. Uhr, J.D. Jamieson and G.E. Palade. 1970. Immunoglobulin synthesis and secretion: II. Radioautographic studies of sites of addition of carbohydrate moieties and intracellular transport. J. Cell Biol. 46:52-63.
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