1973
DOI: 10.1016/0014-4827(73)90119-5
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Anionic sites on the membrane intercalated particles of human erythrocyte ghost membranes. Freeze-etch localization

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Cited by 110 publications
(21 citation statements)
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“…Although the chemical nature of the structures represented by the membrane particles of myelin cannot be established in the present study, investigations of the chemical nature of the particles in other membranes have always revealed that they are protein-containing structures (21)(22)(23)(24)(25).…”
Section: Resultsmentioning
confidence: 76%
“…Although the chemical nature of the structures represented by the membrane particles of myelin cannot be established in the present study, investigations of the chemical nature of the particles in other membranes have always revealed that they are protein-containing structures (21)(22)(23)(24)(25).…”
Section: Resultsmentioning
confidence: 76%
“…However, in these studies membrane skeletons were obtained by Triton extraction of Spectrin-immunogold labelled erythrocytes (unfixed, unglycerinated erythrocyte ghosts and, therefore, did not provide views of the organization of the cytoskeleton associated in situ to the cytoplasmic surface of the erythrocyte membrane. High-resolution, limited views of the inner surface of erythrocyte membrane are provided by freeze-etching of erythrocyte ghosts (13,15,16). Lang et al (8) and Nermut (13) obtained in situ views of the membrane skeleton, after lysis and squirting of erythrocytes attached to positively charged supports.…”
Section: Discussionmentioning
confidence: 99%
“…Although fracture of the bilayer produces smooth faces, in all biological membranes these faces are interrupted by particulate components ("membrane intercalated particles" or "intramembranous particles") and, in most, by subtler rugosities ["subparticles" (5)]. Combined use ofimmunochemical and cytochemical techniques with freeze-etching methods, and freeze-fracture observation of reconstituted membrane preparations, demonstrate that, in the systems used, the particles represent the sites ofintegral transmembrane proteins (6)(7)(8)(9)(10)(11)(12). Because of the qualitative similarity offreeze-fracture images produced by all biological membranes, the particles are assumed to represent local structural asymmetries in the fracture process provoked by integral membrane.proteins and, possibly, their-associated lipids (3,4).…”
mentioning
confidence: 99%
“…Because of the qualitative similarity offreeze-fracture images produced by all biological membranes, the particles are assumed to represent local structural asymmetries in the fracture process provoked by integral membrane.proteins and, possibly, their-associated lipids (3, 4). In the erythrocyte membrane the particles represent the site of the two main integral transmembrane proteins (glycophorin and band III component) which bear AB(H) antigens, influenza virus receptors, wheat germ agglutinin and concanavalin A (Con A) binding sites, as well as anionic sites (8)(9)(10)(11)(13)(14)(15).Although splitting of the bilayer continuum by freeze-fracture (and, in consequence, the partition of peripheral membrane proteins) is established, less is known about the fracture behavior of integral membrane proteins (3, 16)-in particular, their antigens and lectin binding sites at the surface (17). Most particles are generally associated with the inner membrane half (1, 2)-i. e., they are observed on the protoplasmic or P face (18).…”
mentioning
confidence: 99%