Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell.

@article{Pinder1993MembraneAS,
  title={Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell.},
  author={Jennifer Pinder and Amy Chung and Marion E. Reid and Walter B Gratzer},
  journal={Blood},
  year={1993},
  volume={82 11},
  pages={3482-8}
}
The identity of the membrane binding sites for the membrane cytoskeletal protein 4.1 of the human red blood cell has been investigated. Exhaustive proteolysis of the membrane with a range of proteases led to the elimination of only some 60% of all binding sites. The predominant integral membrane protein, band 3, as well as glycophorin A, was totally digested at levels of proteolysis that were essentially without effect on the number of 4.1 binding sites. Proteolysis caused scission of the… CONTINUE READING

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Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell .
Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell .
Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell .
Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell .
The Rh(D ) transmembrane protein , which interacts with the membrane cytoskeleton , is also resistant to proteolysis of the cytoplasmic membrane surface , but Rhnull cells , devoid of this protein , showed no decreased retention of 4.1 .
The Rh(D ) transmembrane protein , which interacts with the membrane cytoskeleton , is also resistant to proteolysis of the cytoplasmic membrane surface , but Rhnull cells , devoid of this protein , showed no decreased retention of 4.1 .
Integral Membrane ProteinsIs biochemical function of gene productGlycophorin A
The predominant integral membrane protein , band 3 , as well as glycophorin A , was totally digested at levels of proteolysis that were essentially without effect on the number of 4.1 binding sites .
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