Cell Fractionation spectrin

Creator:
Marchesi, V
Palade, George E
Published/Created:
New Haven, CT
Yale University School of Medicine
2/2/1967
Physical Description:
3.25 in. x 4 in.
Notes:
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.
Topics:
Cell Fractionation
Topics:
Jamieson, James D
Genre:
transmission electron micrograph
Format:
Image
Content Type:
Prints & Photographs
Rights:
The use of this image may be subject to the copyright law of the United States (Title 17, United States Code) or to site license or other rights management terms and conditions. The person using the image is liable for any infringement
Yale Community Only
Access Restrictions:
Public
Yale Collection:
Yale University School of Medicine, Department of Cell Biology
Digital Collection:
George E. Palade Electron Microscopy Slide Collection
Citation:
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.
OID:
15817833
PID:
digcoll:2795275