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- W2034367443 abstract "1.|A number of different proteins are solubilized from intact haemoglobin-free human and bovine erythrocyte ghosts by dialysis against distilled water followed by a freeze-thaw treatment. 2.|The heterogeneity of the extract is revealed by polyacrylamide gel electrophoresis at pH 8.0, in the absence of dissociating agents. Among the proteins in solution are ones which have quaternary conformations resembling hollow cylinders and single tori. These proteins are identified by electron microscopy. 3.|By analytical ultracentrifugation the sedimentation coefficients of the hollow cylinder and single torus proteins are calculated at 22.5 S and 9.0 S, respectively, at infinite dilution. 4.|The soluble proteins are separated by sucrose density gradient centrifugation. Fractions taken for electrophoresis and electron microscopic study indicate the positioning of the hollow cylinder and torus proteins on the gradient. 5.|The results presented are discussed in relation to those of other workers in the field of erythrocyte membrane proteins." @default.
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- W2034367443 date "1971-03-01" @default.
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- W2034367443 title "Further studies on the proteins released from haemoglobin-free erythrocyte ghosts at low ionic strength" @default.
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- W2034367443 doi "https://doi.org/10.1016/0005-2795(71)90294-7" @default.
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