Lectin binding sites in normal and phenobarbitale/halothane treated rat liver

1989 ◽  
Vol 90 (5) ◽  
pp. 391-397 ◽  
Author(s):  
M. Witt ◽  
Ch. Klessen
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Lectin Binding ◽  
Lectin Binding Sites

scholarly journals Spatial orientation of glycoproteins in membranes of rat liver rough microsomes. I. Localization of lectin-binding sites in microsomal membranes.

1978 ◽  
Vol 78 (3) ◽  
pp. 874-893 ◽  
Author(s):  
E Rodriguez Boulan ◽  
G Kreibich ◽  
D D Sabatini
Keyword(s):  
Endoplasmic Reticulum ◽  
Rat Liver ◽  
Binding Sites ◽  
Microsomal Fraction ◽  
Lectin Binding ◽  
Membrane Glycoproteins ◽  
Con A ◽  
Microsomal Membranes ◽  
Carbohydrate Chains ◽  
Lectin Binding Sites

Carbohydrate-containing structures in rat liver rough microsomes (RM) were localized and characterized using iodinated lectins of defined specificity. Binding of [125I]Con A increased six- to sevenfold in the presence of low DOC (0.04--0.05%) which opens the vesicles and allows the penetration of the lectins. On the other hand, binding of [125I]WGA and [125I]RCA increased only slightly when the microsomal vesicles were opened by DOC. Sites available in the intact microsomal fraction had an affinity for [125I]Con A 14 times higher than sites for lectin binding which were exposed by the detergent treatment. Lectin-binding sites in RM were also localized electron microscopically with lectins covalently bound to biotin, which, in turn, were visualized after their reaction with ferritin-avidin (F-Av) markers. Using this method, it was demonstrated that in untreated RM samples, binding sites for lectins are not present on the cytoplasmic face of the microsomal vesicles, even after removal of ribosomes by treatment with high salt buffer and puromycin, but are located on smooth membranes which contaminate the rough microsomal fraction. Combining this technique with procedures which render the interior of the microsomal vesicles accessible to lectins and remove luminal proteins, it was found that RM membranes contain binding sites for Con A and for Lens culinaris agglutinin (LCA) located exclusively on the cisternal face of the membrane. No sites for WGA, RCA, soybean (SBA) and Lotus tetragonobulus (LTA) agglutinins were detected on either the cytoplasmic or the luminal faces of the rough microsomes. These observations demonstrate that: (a) sugar moieties of microsomal glycoproteins are exposed only on the luminal surface of the membranes and (b) microsomal membrane glycoproteins have incomplete carbohydrate chains without the characteristic terminal trisaccharides N-acetylglucosamine comes from galactose comes from sialic acid or fucose present in most glycoproteins secreted by the liver. The orientation and composition of the carbohydrate chains in microsomal glycoproteins indicate that the passage of these glycoproteins through the Golgi apparatus, followed by their return to the endoplasmic reticulum, is not required for their biogenesis and insertion into the endoplasmic reticulum (ER) membrane.

Lectin-binding sites are found in rat liver cell plasma membrane only on its extracellular surface

1978 ◽  
Vol 29 (1) ◽  
pp. 287-296
Author(s):  
I. Virtanen ◽  
A. Miettinen ◽  
J. Wartiovaara
Keyword(s):  
Rat Liver ◽  
Liver Cell ◽  
Binding Sites ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Surface Membrane ◽  
Ultrastructural Localization ◽  
Cell Plasma ◽  
Extracellular Side ◽  
Lectin Binding Sites

In the present study ultrastructural localization of binding sites for 5 lectins was studied in rat liver cell surface membrane fractions. For this purpose ferritin-coupled Concanavalin A, wheat germ agglutinin, soybean agglutinin, Ricinus communis agglutinin 120 and Lotus tetragonolobus agglutinin I were used as probes for mannose, N-acetyl glucosamine, N-acetyl galactosamine, galactose and fucose moieties in glycoproteins and glycolipids. Although recent reports suggest presence of glycogroups on the cytoplasmic surface of cellular membranes ultrastructural identification of membrane surfaces in the present study indicated an asymmetric localization of lectin-binding sites exclusively on the extracellular side of the membranes.

Lectin-binding sites in chick limb buds

1989 ◽  
Vol 27 ◽  
pp. 82
Author(s):  
M. Narita ◽  
K. Yamashita ◽  
M. Yasuda
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Limb Buds ◽  
Lectin Binding Sites

Ultrastructural demonstration of lectin binding sites in the Golgi apparatus of rat epiphyseal chondrocytes

1988 ◽  
Vol 89 (2) ◽  
pp. 177-184 ◽  
Author(s):  
A. Velasco ◽  
J. Hidalgo ◽  
M. M�ller ◽  
G. Garcia-Herdugo
Keyword(s):  
Golgi Apparatus ◽  
Binding Sites ◽  
Lectin Binding ◽  
Lectin Binding Sites

Photoelectron microscopy of erythrocyte ghosts; imaging of lectin binding sites with colloidal gold markers

1983 ◽  
Vol 12 (3) ◽  
pp. 213-218 ◽  
Author(s):  
G.Bruce Birrell ◽  
Suzanne M. Rose ◽  
O.Hayes Griffith
Keyword(s):  
Binding Sites ◽  
Colloidal Gold ◽  
Lectin Binding ◽  
Erythrocyte Ghosts ◽  
Lectin Binding Sites

Lectin binding sites of the mouse ovary, intraovarian and ovulated ova

1984 ◽  
Vol 80 (6) ◽  
pp. 527-533 ◽  
Author(s):  
T. -C. Wu ◽  
M. -C. Lee ◽  
Y. -J. Wan ◽  
I. Damjanov
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Mouse Ovary ◽  
Lectin Binding Sites

Lectin-binding sites in isolated equine cumulus-oocyte complexes: Differential expression of glycosidic residues in complexes recovered with compact or expanded cumulus

2009 ◽  
Vol 72 (3) ◽  
pp. 300-309 ◽  
Author(s):  
S. Desantis ◽  
G. Ventriglia ◽  
S. Zizza ◽  
T. De Santis ◽  
A. Di Summa ◽  
...  
Keyword(s):  
Differential Expression ◽  
Binding Sites ◽  
Lectin Binding ◽  
Lectin Binding Sites
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