نتایج جستجو برای: succinylated wheat germ agglutinin

تعداد نتایج: 91587  

Journal: :Journal of cell science 1978
I Virtanen A Miettinen J Wartiovaara

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 fu...

2018
Gustavo A Barisone Robert T O'Donnell Yunpeng Ma Mastewal W Abuhay Kathleen Lundeberg Sonia Gowda Joseph M Tuscano

Non-Hodgkin lymphoma (NHL) affects over 400,000 people in the United States; its incidence increases with age. Treatment options are numerous and expanding, yet efficacy is often limited by toxicity, particularly in the elderly. Nearly 70% patients eventually die of the disease. Many patients explore less toxic alternative therapeutics proposed to boost anti-tumor immunity, despite a paucity of...

Journal: :The Journal of biological chemistry 1991
S Rens-Domiano T Reisine

SRIF receptors are membrane-bound glycoproteins. To structurally identify the carbohydrate components of SRIF receptors, solubilized rat brain SRIF receptors were subjected to lectin affinity chromatography. Solubilized SRIF receptors specifically bound to wheat germ agglutinin-lectin affinity columns but not to succinylated wheat germ agglutinin. This finding, as well as the ability of the sol...

Journal: :The Journal of Cell Biology 1982
P P da Silva M R Torrisi

Thin-section and critical-point-dried fracture-labeled preparations are used to determine the distribution and partition of glycophorin-associated wheat germ agglutinin (WGA) binding sites over protoplasmic and exoplasmic faces of freeze-fractured human erythrocyte membranes. Most wheat germ agglutinin binding sites are found over exoplasmic faces. Label is sparse over the protoplasmic faces. T...

Journal: :The Journal of Cell Biology 1983
A M Tartakoff P Vassalli

We investigated the subcellular sites of glycoprotein oligosaccharide maturation by using lectin conjugates to stain lightly-fixed, saponin-permeabilized myeloma cells. At the electron microscopic level, concanavalin A-peroxidase stains the cisternal space of the nuclear envelope, the rough endoplasmic reticulum, and cisternae along the proximal face of the Golgi stack. Conversely, wheat germ a...

2003
RONALD J. DOYLE F. NEDJAT-HAIEM E. FRASCH

The lectin slide agglutination test for Neisseria gonorrhoeae has been modified and improved. Results show that wheat germ agglutinin and soybean lectin agglutinate 100% (193 of 193 tested) of clinical isolates of N. gonorrhoeae. Lectin-reactive meningococci can be readily identified by the hydrolysis of gammaglutamyl-3-naphthylamide. Branhamella catarrhalis, Neisseria lactamica, Neisseria sicc...

Journal: :The Journal of Cell Biology 1984
A P Aguas P Pinto da Silva

Membrane halves of boar sperm flagella were produced by freeze-fracture and labeled in situ with concanavalin A and wheat germ agglutinin; the lectins were visualized with protein-gold complexes. Concanavalin A and wheat germ agglutinin binding sites partition with both protoplasmic and exoplasmic halves of the membrane. A high density of lectin marking was found on protoplasmic membrane halves...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1974
J T Lamont J L Perrotto M M Weiser K J Isselbacher

Lectin agglutination and cell surface galactosyltransferase (EC 2.4.1.67; 1-O-alpha-D-galactosyl-myo-inositol:raffinose galactosyltransferase) enzyme activity have been studied with thymus and spleen lymphocytes of neonatal rats. Thymus lymphocytes were more agglutinable by concanavalin A than by wheat germ agglutinin, whereas spleen lymphocytes were more agglutinable by wheat germ agglutinin t...

Journal: :Biochemical Society transactions 1990
D MacEwan R Mitchell

D,-dopamine receptors extracted from bovine caudate nucleus, using the detergent cholate, have been purified to apparent homogeneity by affinity chromatography on haloperidol-Sepharose and wheat-germ agglutinin-agarose columns [ 11. In this report, we describe a preliminary comparison of purified receptor preparations derived from other D,-dopamine-receptor-rich regions of bovine brain and the ...

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