scholarly journals Labelling of the intramembranous region of the major sialoglycoprotein of human erythrocytes with a photosensitive hydrophobic probe

1979 ◽  
Vol 179 (2) ◽  
pp. 265-272 ◽  
Author(s):  
E Wells ◽  
J B Findlay
Keyword(s):  
Membrane Proteins ◽  
Human Erythrocyte ◽  
Human Erythrocytes ◽  
Labelling Pattern ◽  
Erythrocyte Membranes ◽  
Transmembrane Region ◽  
Human Erythrocyte Membranes ◽  
Hydrophobic Probe

Human erythrocyte membranes were incubated with the photosensitive hydrophobic reagent 1-azido-r-iodo[3H]benzene and the mixture was irradiated. The major sialoglycoprotein was then isolated and the labelled polypeptide subjected to proteolytic dissection. Characterization of the purified tryptic and chymotryptic peptides show that the probe is covalently attached only to the transmembrane region of the protein. This labelling pattern is discussed in relation to the use of such reagents for the identification of segments of membrane proteins exposed to the hydrophobic millieu of the membrane.

scholarly journals Membrane glycopeptides from old and young human erythrocytes (Short Communication)

1974 ◽  
Vol 140 (3) ◽  
pp. 557-560 ◽  
Author(s):  
Cesare Balduini ◽  
Carlo Luigi Balduini ◽  
Edoardo Ascari
Keyword(s):  
Sialic Acid ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Short Communication ◽  
Chemical Characterization ◽  
Erythrocyte Membranes ◽  
Main Peak ◽  
Human Erythrocyte Membranes ◽  
Papain Digestion

Glycopeptides were extracted by papain digestion from old and young human erythrocyte membranes and fractionated on DEAE-Sephadex A-25. Chemical characterization of the unfractionated samples and of the main peak eluted from the column indicates that glycoproteins of the erythrocyte membrane undergo significant decreases in sialic acid and galactosamine content with aging.

Characterization of A (Ca2+ + Mg2+)-ATPase activator bound to human erythrocyte membranes

Cell Calcium ◽  
1984 ◽  
Vol 5 (1) ◽  
pp. 77-88 ◽  
Author(s):  
Basil D. Roufogalis ◽  
Christine T. Elliott ◽  
Gregory B. Ralston
Keyword(s):  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes

scholarly journals Expression of the major sialoglycoprotein (glycophorin) on erythroid cells in human bone marrow

Blood ◽  
1978 ◽  
Vol 52 (2) ◽  
pp. 379-387 ◽  
Author(s):  
CG Gahmberg ◽  
M Jokinen ◽  
LC Andersson
Keyword(s):  
Bone Marrow ◽  
Membrane Proteins ◽  
Cell Surface ◽  
Human Erythrocyte ◽  
Bone Marrow Cells ◽  
Protein A ◽  
Human Bone ◽  
Erythrocyte Membranes ◽  
Erythroid Cells ◽  
Human Erythrocyte Membranes

The major sialoglycoprotein of human erythrocyte membranes (glycophorin) is one of the most-studied membrane proteins. Although the structure is relatively well known, almost nothing is known about its expression in erythroid cells. To study this we raised an antiserum that reacted specifically with this protein. This was accomplished by immunization of rabbits with a preparation of glycophorin followed by absorption with En(a-) erythrocyte membranes, which lack glycophorin. By use of this antiserum and a staphylococcus protein A technique we could establish that only bone marrow cells of erythrocyte lineage express glycophorin at the cell surface. This occurs in basophilic normoblasts and later stages of erythrocyte differentiation, whereas pronormoblasts do not seem to contain glycophorin.

Freeze-fracture Electron Microscopic observations on the effects of sulphydryl group reagents on human erythrocyte membranes

1990 ◽  
Vol 48 (3) ◽  
pp. 524-525 ◽  
Author(s):  
Gheorghe Benga ◽  
Anthony Brain ◽  
Victor I. Pop ◽  
John Wrigglesworth
Keyword(s):  
Human Erythrocyte ◽  
Freeze Fracture ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Electron Microscopic ◽  
Experimental Conditions ◽  
Water Permeation ◽  
Human Erythrocyte Membranes ◽  
Erythrocyte Membrane Proteins

The intra-membrane particles (IMPs) observed on the fracture face of frozen erythrocyte membranes are thought to correspond primarily to “band 3” tetramers or dimers. Some recent studies correlating the inhibition of water diffusion in erythrocytes by p-chloromercuribenzene sulfonate (PCMBS) with the binding of 203Hg to erythrocyte membrane proteins has enabled band 3 and the polypeptides in band 4.5 to be identified as the proteins associated with the channels for water permeation in human erythrocytes. A further characterization of the effects of the incubation of human erythrocyte membranes with PCMBS and N-ethylmaleimide (NEM) has been performed as previously described. Experimental conditions have been previously described.A comparison was made of the appearance of freeze-etched membranes of control erythrocytes and erythrocytes with the sulphydryl reagents. It was found that on many of the control and NEM-treated cells, small (50-100 nm) elevated patches could be seen (Fig. 1, 2 and 3). These are present on both fracture and etch faces and are devoid of any intramembrane particles. The patch elevations were never observed in the membranes of PCMBS-treated cells (Fig. 4).

Evidence against the Involvement of Mutarotase in the D-Glucose Uptake Activity of Isolated Human Erythrocyte Membranes

1972 ◽  
Vol 50 (9) ◽  
pp. 1028-1030 ◽  
Author(s):  
Arthur Kahlenberg ◽  
Gary Miller
Keyword(s):  
Glucose Uptake ◽  
Membrane Transport ◽  
Glucose Transport ◽  
Human Erythrocyte ◽  
Transport Process ◽  
Human Erythrocytes ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes ◽  
Uptake Activity ◽  
Glucose Carrier

Mutarotase, the enzyme catalyzing the interconversion of the anomeric forms of D-glucose, has recently been suggested to be the membrane glucose carrier in human erythrocytes. However, hemoglobin-free human erythrocyte membranes possessing D-glucose uptake activity were found to be free of mutarotase activity. Mutarotase activity was detected in the membrane-free hemolysates of the cells. It is therefore concluded that the D-glucose uptake activity of isolated erythrocyte membranes is not due to the binding of the sugar to mutarotase, and that this enzyme is not involved in glucose transport in a manner compatible with most presently held concepts of the membrane transport process.

Characterization of a Monoclonal Antibody Against P57, The C3/C3b-Cleaving Proteinase Expressed in Human Erythrocyte Membranes

Hybridoma ◽  
1991 ◽  
Vol 10 (4) ◽  
pp. 449-458 ◽  
Author(s):  
ANNY FIANDINO-TIREL ◽  
MONIQUE BAREL ◽  
FOUAD LYAMANI ◽  
ALINE GAUFFRE ◽  
JACQUES HERMANN ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes
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