The structure of erythrocyte spectrin in negatively stained membrane skeletons
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The structure of erythrocyte spectrin in negatively stained membrane skeletons

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Published .
Written in English


Book details:

Edition Notes

Statementby Amy Marie McGough.
Classifications
LC ClassificationsMicrofilm 93/552 (Q)
The Physical Object
FormatMicroform
Paginationviii, 191 leaves
Number of Pages191
ID Numbers
Open LibraryOL1050683M
LC Control Number93629776

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the skeleton, spectrin is a straight molecule that does not display a well-defined structure. However, by using condi-tions closer to the physiological range, it is possible to obtain micrographs of skeletons that are partially expanded. In the work described below we have examined electron micro-graphs of negatively stained spectrin molecules that are. The structure of the membrane skeleton on the cytoplasmic surface of the erythrocyte plasma membrane was observed in dried human erythrocyte ghosts by atomic force microscopy (AFM), taking advantage of its high sensitivity to small height variations in by: We have studied the structure of negatively stained spectrin in partially expanded membrane skeletons to determine how its molecular structure confers elastic properties on the cell membrane. intact erythrocyte membrane skeleton were obtained by negative staining(1, 2), in onlyonemicrographpublishedby Pinder et al. (12) can one see individual spectrin tetramers and fragmentary hints ofthe band actin oligomerjunc-tions. Wehave now obtained clear images of the spectrin meshwork from negatively stained preparations that origi-Cited by:

loss of membrane lipid, and increased tendency for affected erythrocytes to fuse The surface area of the erythrocyte skeleton appears to be larger than necessary to cover the inner surface of the erythrocyte. Theoretical calculations indicate that spectrin molecules may be 3 times longer than. a modeP 6 of the erythrocyte membrane as a visco. elastic protein-lipid gel, and with a threefold increase in the linear dimensions of the membrane skeleton during spreadinglZ. Compact spectrin molecules are also apparent in samples of mem- brane skeletons examined by negative staining at.   Figure ew of the membrane-associated periodic skeleton (MPS) of neurons and its associated proteins. (A) The MPS abundance and organization in different domains of a neuron, from being robust and well organized in the axon initial segment to being completely absent in the cell soma.(B) Axon shafts from sensory neurons in culture, stained against βII-spectrin and imaged by Cited by: FORUM A model of spectrin as a concertina in. the erythrocyte membrane skeleton To maintain its distinctive biconcave shape, the erythrocyte has a skeleton composed largely of the protein spectrin, which associates closely and exclusively with the cell by:

Localization and Structure of the Ankyrin-binding Site on 2-Spectrin erythrocyte membrane skeleton from negatively stained preparations that originate directly from the intact cell but in.   Cohen, CM, Langley, RC, Foley, SF, Korsgren, C: Functional associations of band in the erythrocyte membrane skeleton and their role in inherited membrane skeletal abnormalities. Prog Clin Biol Res 13 – 29, Cited by:   Filamentous skeletons were liberated from isolated human erythrocyte membranes in Triton X, spread on fenestrated carbon films, negatively stained, and viewed intact and unfixed in the transmission electron microscope. Two forms of the skeleton were. We have obtained clear images of the erythrocyte membrane skeleton from negatively stained preparations that originate directly from the intact cell but in which the spectrin meshwork is artificially spread to allow close inspection. Our procedure requires Cited by: