3.25 in. x 4 in. Lantern Slides Original Magnification: x25,000 Dr. V. T. Marchesi from Yale and colleagues took advantage of the high purity of red cell ghosts obtained by hypotonic lysis to analyze the properties of membrane proteins. They identified spectrin (from the Latin specere, to look at - or ghost) as a major red cell membrane cytoskeletal protein responsible for maintaining the biconcave shape of red cells. In hereditary spherocytosis, spectrin is mutated resulting in anemias due to greater fragility of red cells which cannot assume a biconcave shape.
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 Marchesi, V.T. and G.E. Palade. 1967. The localization of Mg-Na-K-activated adenosine triphosphatase on red cell ghost membranes. J. Cell Biol. 35:385-404. Nicoloson, G.L., V.T. Marchesi and S.J. Singer. 1971. The localization of spectrin on the inner surface of human red blood cell membranes by ferritin-conjugated antibodies. J. Cell Biol. 51:265-272. Marchesi, V.T. and E. Steers, Jr. 1968. Selective solubilization of a protein component of the red cell membrane. Science. 159:203-204.
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