Results 91 to 100 of about 135 (130)

Concanavalin A receptor capping in mouse myeloma and hybridoma

Cell Biology International Reports, 1986
Concanavalin A capping was studied in immunoglobulin-secreting hybridomas derived from fusion of mouse myeloma NSO cells with mouse spleen lymphocytes. The cells of the parental populations differed significantly in capping ability (low in myeloma cells and high in the lymphocytes).
A, Staroselsky, L, Peleg, E, Levitov, H, Slor, N S, Kosower   +4 more
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Mobility of Concanavalin a Receptors in Myelin and Synaptic Membranes

Nature New Biology, 1973
THERE is now abundant evidence that biological membranes are fluid in nature with constituent protein and lipid molecules able to move relative to one another in the plane of the membrane1–6. In cells that occur in the unassociated state such as lymphocytes, surface macromolecules appear to be randomly distributed in the membrane unless cross linked by
A, Matus, S, De Petris, M C, Raff
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Microtubular Proteins and Concanavalin A Receptors

1975
The inherent topographical distribution of Con A binding sites (CABS) is disperse or random in all cell types studied using hemocyanin to mark CABS in surface replicas. In virally transformed cells, the addition of Con A leads to the formation of clusters (CABS).
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Are Concanavalin A Receptor Sites Mediators of Cell-Cell Adhesion?

Nature New Biology, 1973
THE identity of the chemical sites that mediate adhesions between tissue cells remains to be established. Attractive candidates for this role include carbohydrate-containing groups which have in recent years been shown to be common structural constituents of animal cell membranes1.
M S, Steinburg, I A, Gepner
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Cytoskeletal control of concanavalin A receptor mobility in peritoneal macrophages

Experimental Cell Research, 1979
Abstract The role of microtubules and microfilaments in controlling the mobility of concanavalin A (ConA) receptors in the membrane of peritoneal macrophages was examined. Receptor mobility was assessed by counting the number of cells exhibiting cap formation following incubation with fluorescein-labelled ConA for 5 min at 37 °C.
E, Pick, I, Wilner
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The distribution of concanavalin a receptor sites on the membrane of chromaffin granules

Journal of Cell Science, 1975
ABSTRACT The distribution of concanavalin A (con A) receptor sites on the membranes of chromaffin granules has been investigated by binding studies using 125I-labelled con A and by electron-microscope studies using ferritin-labelled con A.
P A, Eagles, L N, Johnson, C, Van Horn
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Immobilization of concanavalin A receptors during differentiation of neuroblastoma cells

Nature, 1981
Neuroblastoma cells serve as a useful model of neuronal development because compounds such as dimethyl sulphoxide (DMSO) and dibutyryl cyclic AMP cause them to undergo a process of controlled differentiation in tissue culture, during which they can extend long processes, develop characteristic excitability mechanisms, synthesize neurotransmitters and ...
M C, Fishman, P R, Dragsten, I, Spector
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Isolation of a concanavalin A receptor from mouse L cells

Biochemistry, 1975
A cell surface glycoprotein receptor for concanavalin A (Con A) has been isolated from mouse L cells. The isolation procedure involved dissolving whole L cells in 0.3 M lithium diiodosalicylate and extracting with aqueous phenol. The Con A receptor, which was found in the aqueous phase of this extract, was further purified by affinity chromatography on
R C, Hunt, C M, Bullis, J C, Brown
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Dynamic state of concanavalin a receptor interactions on fibroblast surfaces

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1975
Cultured normal and transformed fibroblasts were treated "in situ" by the concanavalin A-peroxidase labelling technique. It is known that peroxidase recognizes only a fraction of the bound lectin depending on the cell type. Kinetics studies revealed that 80 to 95 percent of the peroxidase and only 10 percent of the lectin are released from the cell ...
C, Huet, A, Bernadac
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Interaction between the hepatic growth hormone receptor and concanavalin A

Molecular and Cellular Endocrinology, 1979
The interaction between the plant lectin concanavalin A (Con A) and hepatic receptors for human growth hormone (GH) has been studied in particulate and soluble microsomal membrane preparations from rabbit and rat liver. Con A shows a dose-dependent, partial (30%) inhibition of 125I-human GH binding which is reversed by the Con A competitor, alpha ...
A C, Herington, D, Elson
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