scholarly journals Localization of Wheat Germ Agglutinin Lectin Receptors on Human Sperm by Fluorescence Microscopy: Utilization of Different Fixatives

1994 ◽  
Vol 33 (2) ◽  
pp. 77-85 ◽  
Author(s):  
L. K. Gabriel ◽  
D. R. Franken ◽  
G. Van Der Horst ◽  
T. F. Kruger
Keyword(s):  
Fluorescence Microscopy ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Human Sperm ◽  
Lectin Receptors ◽  
Wheat Germ Agglutinin Lectin

scholarly journals Lateral diffusion in nuclear membranes.

1985 ◽  
Vol 100 (5) ◽  
pp. 1408-1414 ◽  
Author(s):  
M Schindler ◽  
J F Holland ◽  
M Hogan
Keyword(s):  
Diffusion Coefficient ◽  
Outer Membrane ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Lipid Analysis ◽  
Membrane Integrity ◽  
Lateral Diffusion ◽  
Protein Diffusion ◽  
Inner Membrane ◽  
Lectin Receptors

Chemical modification of rat liver nuclei with citraconic anhydride selectively removed outer nuclear membrane. This conclusion was based on (a) transmission electron microscopy, (b) lipid analysis, (c) lamin B as an inner membrane-associated marker, and (d) the demonstration of phospholipid lateral mobility on outer membrane-depleted nuclei as a criteria for inner membrane integrity. Addition of urea or N-ethylmaleimide resulted in the additional disruption of inner membrane. Fluorescence photobleaching was used to determine the long range (greater than 4 microns) lateral transport of lectin receptors and a phospholipid analog in both membranes. The diffusion coefficient for wheat germ agglutinin on whole nuclei was 3.9 X 10(-10) cm2/s whereas the diffusion coefficient for wheat germ agglutinin in outer membrane-depleted nuclei was less than or equal to 10(-12) cm2/s. Phospholipid mobilities were the same in whole and outer membrane-depleted nuclei (3.8 X 10(-9) cm2/s). The protein diffusion differences observed between whole and outer membrane-depleted nuclei may be interpreted in the context of two functionally different membrane systems that compose the double bilayer of the nucleus.

scholarly journals Quantitation of lectin binding sites in human colon mucins by use of peanut and wheat germ agglutinins.

1988 ◽  
Vol 36 (10) ◽  
pp. 1305-1307 ◽  
Author(s):  
C R Boland ◽  
J A Roberts
Keyword(s):  
Colon Cancer ◽  
Fluorescence Microscopy ◽  
Binding Sites ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Lectin Binding ◽  
Human Colon ◽  
Peanut Agglutinin ◽  
Normal Colon ◽  
Lectin Binding Sites

We have developed a novel method for quantitation of lectin binding sites in mucins derived from colon tissues. Binding of peanut agglutinin and wheat germ agglutinin was measured in extracts from normal and malignant human colon epithelium. Binding of wheat germ agglutinin was used as an estimate of the total mucin present in the tissue extract. Peanut agglutinin was found to bind to mucin from normal colon, but at levels that may be difficult to appreciate by fluorescence microscopy. The yield of mucin extracted from colon cancer was more variable than that from normal colon, and the binding ratio of peanut agglutinin to wheat germ agglutinin was greater in extracts from tumors than in normal tissues. Our findings confirm the histological observation that peanut agglutinin binds more avidly to mucins from colon cancer than to those from normal colon. The finding of peanut agglutinin binding sites in mucins front normal colon was not expected. The quantitative technique may have detected small numbers of binding sites not readily appreciable by fluorescence microscopy. Alternatively, the chromatographic method for measuring lectin binding may be sufficiently sensitive to detect nonspecific binding of the lectin to terminal galactose residues other than the Thomsen-Friedenreich antigen.

Wheat germ agglutinin receptors on human sperm membranes and sperm morphology

Andrologia ◽  
2009 ◽  
Vol 26 (1) ◽  
pp. 5-8 ◽  
Author(s):  
L. K. Gabriel ◽  
D. R. Franken ◽  
G. Horst ◽  
T. F. Kruger ◽  
S. C. Oehninger
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Sperm Morphology ◽  
Human Sperm

Concanavalin a and Wheat Germ Agglutinin Receptors in the Ascitic Fluid of Rat Hepatomas

1979 ◽  
Vol 65 (1) ◽  
pp. 9-18 ◽  
Author(s):  
Giovanni Neri ◽  
Shelley Palmer Hayes ◽  
Harilyn W. Smith ◽  
Sylvia Capetillo ◽  
Earl F. Walborg
Keyword(s):  
Ascitic Fluid ◽  
Concanavalin A ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Hepatoma Cell ◽  
Hepatoma Cells ◽  
Receptor Activity ◽  
Con A ◽  
Novikoff Hepatoma ◽  
Lectin Receptors

The presence of glycopeptide lectin receptors in the ascitic fluid of rats bearing Novikoff or AS-30D hepatoma was investigated. Macrosialoglycopeptides, resistant to pronase digestion, were partially purified from the ascitic fluid of hepatoma-bearing rats by gel filtration on Sephadex G-50. A macrosialoglycopeptide fraction, isolated from the ascitic fluid of rats bearing the Novikoff hepatoma, possessed potent concanavalin A (Con A) receptor activity. This fraction possessed higher Con A receptor activity than did the comparable macrosialoglycopeptide fraction from the ascitic fluid of rats bearing the AS-30D hepatoma; this observation is in agreement with the Con A-induced agglutination properties of these 2 hepatoma cell lines and with the Con A receptor activities of the glycopeptides released from the surface of the hepatoma cells by papain digestion. Rat blood serum contained a comparable macrosialoglycopeptide fraction, which possessed weak Con A receptor activity. The macrosialoglycopeptide fractions from the ascitic fluid of hepatoma-bearing rats possessed wheat germ agglutinin receptor activity. However, this activity was also present in normal rat serum. These results suggest that glycopeptides present on the surface of Novikoff hepatoma cells are shed into the ascitic fluid and may be distinguished from components in normal serum by their Con A receptor activity.

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