Ultrastructural localization of Helix pomatia lectin-binding sites in mouse lung elastic fibers

1987 ◽  
Vol 88 (1) ◽  
pp. 91-95 ◽  
Author(s):  
K. C. Palmer ◽  
L. A. Bale
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Helix Pomatia ◽  
Ultrastructural Localization ◽  
Mouse Lung ◽  
Elastic Fibers ◽  
Helix Pomatia Lectin ◽  
Lectin Binding Sites

scholarly journals Ultrastructural localization of lectin-binding sites on the zonae pellucidae and plasma membranes of mammalian eggs.

1975 ◽  
Vol 66 (2) ◽  
pp. 263-274 ◽  
Author(s):  
G L Nicolson ◽  
R Yanagimachi ◽  
H Yanagimachi
Keyword(s):  
Binding Sites ◽  
Plasma Membranes ◽  
Ricinus Communis ◽  
Lectin Binding ◽  
Ultrastructural Localization ◽  
Con A ◽  
Plasma Membrane Receptor ◽  
Rat Eggs ◽  
Mammalian Eggs ◽  
Lectin Binding Sites

Receptors for Ricinus communis agglutinin I (RCAI), concanavalin A (Con A), and wheat germ agglutinin (WGA) were localized on the zonae pellucidae and plasma membranes of hamster, mouse, and rat eggs with ferritin-lectin conjugates. Intact eggs labeled with the ferritin conjugates showed dense concentrations of RCAI and WGA receptors in the outermost regions of their zonae pellucidae and sparse distributions of Con A receptors throughout the zonae. Ferritin-lectin labeling was specific, since inhibitory saccharides effectively blocked labeling. The asymmetric density of RCAI receptors across the zona was confirmed by ferritin-RCAI and fluorescein-RCAI labeling of mechanically isolated zonae pellucidae, indicating that the RCAI-binding sites are more densely distributed in the exterior zona regions. Plasma membranes of rodent eggs contained RCAI, WGA, and Con A receptors. These receptors were found to be more or less randomly distributed on surfaces of aldehyde-fixed eggs or on eggs labeled near 0 degrees C. However, eggs incubated at 25 degrees C showed aggregated WGA- and Con A-binding site distributions on their plasma membranes. This indicates that lectin-induced receptor redistribution occurs at this temperature. The possibility that plasma membrane receptor mobility is a requirement for sperm-egg fusion is discussed.

Ultrastructural localization of lectin-binding sites in different basement membranes

1993 ◽  
Vol 25 (6) ◽  
pp. 464-468 ◽  
Author(s):  
Mehrdad Salamat ◽  
Werner G�tz ◽  
J�rgen Werner ◽  
Rainer Merken
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Ultrastructural Localization ◽  
Basement Membranes ◽  
Lectin Binding Sites

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.

scholarly journals Peroxidase and gold complexes of lectins for double labeling of surface-binding sites by electron microscopy.

1977 ◽  
Vol 25 (10) ◽  
pp. 1181-1184 ◽  
Author(s):  
J Roth ◽  
M Wagner
Keyword(s):  
Electron Microscopy ◽  
Horseradish Peroxidase ◽  
Concanavalin A ◽  
Binding Sites ◽  
Lectin Binding ◽  
Helix Pomatia ◽  
Surface Binding ◽  
Double Labeling ◽  
Membrane Bound ◽  
Lectin Binding Sites

Double labeling experiments were performed for visualization of the binding sites of Concanavalin A and anti-AHel (the lectin from Helix pomatia). The anti-AHel was labeled with the colloidal gold whereas the membrane bound Concanavalin A was demonstrated by an affinity technique using horseradish peroxidase. The two markers used could be clearly distinguished electron microscopically. The specificity of the cell surface double labeling was demonstrated in the control experiments. A topological distinct localization of the both lectin-binding sites is evident.

Ultrastructural localization of lectin binding sites in the developing brain microvasculature

1998 ◽  
Vol 197 (4) ◽  
pp. 305-315 ◽  
Author(s):  
B. Nico ◽  
Fabio Quondamatteo ◽  
Domenico Ribatti ◽  
Mirella Bertossi ◽  
Giangiuseppe Russo ◽  
...  
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Ultrastructural Localization ◽  
Developing Brain ◽  
Brain Microvasculature ◽  
Lectin Binding Sites
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