scholarly journals Membrane Protein Transfer from Human Erythrocyte Ghosts to Liposomes Containing an Artificial Boundary Lipid.

1995 ◽  
Vol 71 (3) ◽  
pp. 93-97 ◽  
Author(s):  
Ken-ichi SUZUKI ◽  
Yukihisa OKUMURA ◽  
Toshinori SATO ◽  
Junzo SUNAMOTO
Keyword(s):  
Membrane Protein ◽  
Human Erythrocyte ◽  
Erythrocyte Ghosts ◽  
Protein Transfer ◽  
Artificial Boundary

scholarly journals INTRAMEMBRANE PARTICLE AGGREGATION IN ERYTHROCYTE GHOSTS

1974 ◽  
Vol 63 (3) ◽  
pp. 1018-1030 ◽  
Author(s):  
Arnljot Elgsaeter ◽  
Daniel Branton
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Particle Aggregation ◽  
Erythrocyte Ghosts ◽  
Intramembrane Particle ◽  
Freeze Etching ◽  
Human Erythrocyte Ghost

We have used freeze-etching and SDS-polyacrylamide gel electrophoresis to study the conditions under which the intramembrane particles of the human erythrocyte ghost may be aggregated. The fibrous membrane protein, spectrin, can be almost entirely removed from erythrocyte ghosts with little or no change in the distribution of the particles. However, after spectrin depletion, particle aggregation in the plane of the membrane may be induced by conditions which cause little aggregation in freshly prepared ghosts. This suggests that the spectrin molecules form a molecular meshwork which limits the translational mobility of the erythrocyte membrane particles.

The Phosphorus Components of Solubilized Erythrocyte Membrane Protein

1971 ◽  
Vol 49 (3) ◽  
pp. 337-347 ◽  
Author(s):  
F. B. St. C. Palmer ◽  
J. A. Verpoorte
Keyword(s):  
Sialic Acid ◽  
Membrane Protein ◽  
Organic Solvents ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Gel Electrophoresis ◽  
Electrophoretic Pattern ◽  
Erythrocyte Ghosts ◽  
Butanol Extraction ◽  
Chloroform Methanol

Membrane protein preparations were obtained by n-butanol extraction of salt-free aqueous suspensions of human erythrocyte ghosts. The solubilized protein contained 4.5% carbohydrate, including glucosamine and galactosamine, 1.7% sialic acid, and 0.2% phosphorus. Gel electrophoresis indicated the presence of a large number of proteins in the solubilized fraction. Of the phosphorus present 15% could be extracted with chloroform–methanol (2/1) and was shown to consist of phosphatidylserine and some phosphatidylinositol. A further 65% of the phosphorus was extracted with chloroform–methanol–HCl (200/100/1) and this extract was shown to consist principally of diphosphoinositide and triphosphoinositide. The remaining protein-bound phosphorus, representing 0.03% of the protein, could not be separated from the protein. Following treatment with the organic solvents the protein was resolubilized. The carbohydrate and sialic acid concentrations and the gel electrophoretic pattern were not altered. Following incubation of erythrocytes with inorganic 32P, the polyphosphoinositides were rapidly labelled. The phosphoprotein was also rapidly labelled but to a lesser extent. The phosphatidylinositol and phosphatidylserine were very poorly labelled.

scholarly journals The organization of the major protein of the human erythrocyte membrane

1974 ◽  
Vol 137 (3) ◽  
pp. 531-534 ◽  
Author(s):  
D. H. Boxer ◽  
R. E. Jenkins ◽  
M. J. A. Tanner
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Intact Cell ◽  
The Other ◽  
Major Protein ◽  
Erythrocyte Ghosts ◽  
Human Erythrocyte Membrane ◽  
Cytoplasmic Surface ◽  
Peptide Maps

The enzyme lactoperoxidase was used to catalyse the radioiodination of membrane proteins in intact human erythrocytes and in erythrocyte ‘ghosts’. Two major proteins of the erythrocyte membrane were isolated after iodination of these two preparations, and the peptide ‘maps’ of each protein so labelled were compared. Peptides from both proteins are labelled in the intact cell. In addition, further mobile peptides derived from one of the proteins are labelled only in the ‘ghost’ preparation. Various sealed ‘ghost’ preparations were also iodinated, lactoperoxidase being present only at either the cytoplasmic or extra-cellular surface of the membrane. The peptide ‘maps’ of protein E (the major membrane protein) labelled in each case were compared. Two discrete sets of labelled peptides were consistently found. One group is obtained when lactoperoxidase is present at the extra-cellular surface and the other group is found when the enzyme is accessible only to the cytoplasmic surface of the membrane. The results support the assumption that the organization of protein E in the membrane of the intact erythrocyte is unaltered on making erythrocyte ‘ghosts’. They also confirm previous suggestions that both the sialoglycoprotein and protein E extend through the human erythrocyte membrane.

Lead and calcium transport in human erythrocyte

1999 ◽  
Vol 18 (5) ◽  
pp. 327-332 ◽  
Author(s):  
J V Calderón-Salinas ◽  
M A Quintanar-Escorcia ◽  
M T González-Martínez ◽  
C E Hernández-Luna
Keyword(s):  
Transport System ◽  
Human Erythrocyte ◽  
Calcium Transport ◽  
Human Erythrocytes ◽  
The Other ◽  
Erythrocyte Ghosts ◽  
Passive Transport ◽  
Ca Uptake

In this paper we report the lead (Pb) and calcium (Ca) uptake by erythrocyte ghosts. In both cases the transport was carried out by a passive transport system with two kinetic components (Michaelis-Menten and Hill). Pb and Ca were capable of inhibiting the transport of the other metal in a non-competitive way. Under hyperpolarization, the uptakes of Ca and Pb were enhanced and the Michaelis-Menten component prevailed. Both Ca and Pb uptakes were inhibited by N-ethyl-maleimide to the same extent. These results indicate that Pb and Ca share the same permeability pathway in human erythrocytes and that this transport system is electrogenic.

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