Effects of surface proteins of human erythrocyte membrane on the interaction with lipopolysaccharides from Escherichia coli O55:B5

2008 ◽  
Vol 2 (2) ◽  
pp. 128-132 ◽  
Author(s):  
D. S. Kabanov ◽  
A. Yu. Ivanov ◽  
M. Melzer ◽  
I. R. Prokhorenko
Keyword(s):  
Escherichia Coli ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Surface Proteins ◽  
Human Erythrocyte Membrane

scholarly journals Appearance and distribution of surface proteins of the human erythrocyte membrane. An electron microscope and immunochemical labeling study.

1978 ◽  
Vol 76 (2) ◽  
pp. 512-531 ◽  
Author(s):  
D Shotton ◽  
K Thompson ◽  
L Wofsy ◽  
D Branton
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Indirect Evidence ◽  
Surface Proteins ◽  
Human Erythrocyte Membrane ◽  
Intramembrane Particle ◽  
Translational Movement ◽  
Cytoplasmic Surface ◽  
Particle Aggregates ◽  
Before And After

We have used freeze-etching, before and after immunoferritin labeling, to visualize spectrin molecules and other surface proteins of the human erythrocyte membrane. After intramembrane particle aggregation was induced, spectrin molecules, identified by labeling with ferritin-conjugated antispectrin, were clustered on the cytoplasmic surface of the membrane in patches directly underlying the particle clusters. This labeling pattern confirms the involvement of spectrin in such particle aggregates, as previously inferred from indirect evidence. Ferritin-conjugated antihapten molecules, directed against external and cytoplasmic surface proteins of the erythrocyte membrane which had been covalently labeled nonspecifically with the hapten p-diazoniumphenyl-beta-D-lactoside, were similarly found in direct association with such intramembrane particle aggregates. This indicates that when spectrin and the intramembrane particles are aggregated, all the major proteins of the erythrocyte membrane are constrained to coaggregate with them. Although giving no direct information concerning the freedom of translational movement of proteins in the unperturbed erythrocyte membrane, these experiments suggest that a close dynamic association may exist between the integral and peripheral protein components of the membrane, such that immobilization of one component can restrict the lateral mobility of others.

scholarly journals A Ceramide Pentasaccharide of Human Erythrocyte Membrane

1974 ◽  
Vol 249 (4) ◽  
pp. 1022-1025
Author(s):  
Klaus Stellner ◽  
Sen-Itiroh Hakomori
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane

Permeability of the Human Erythrocyte Membrane to Xylitol

1970 ◽  
Vol 12 (1) ◽  
pp. 65-65
Author(s):  
Yuko Yamada ◽  
Hisashi Yamada ◽  
Minoru Hamada
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane

Effect of acylphosphatase on human erythrocyte membrane Ca2+-ATPase

1990 ◽  
Vol 168 (2) ◽  
pp. 651-658 ◽  
Author(s):  
P. Nassi ◽  
C. Nediani ◽  
G. Liguri ◽  
N. Taddei ◽  
M. Ruggiero ◽  
...  
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane
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