منابع مشابه
BINDING SITES ON CONCANAVALIN A 399 Concanavalin
Equilibrium dialysis of concanavalin A against methyl c¢-D-mannopyranoside and methyl C¢-D-glucopyranoside conducted at 2 ° in the presence of I M NaC1 showed that concanavalin A is bivalent. A SCATCHARD plot of the data obtained gave straight lines for both sugars with observed association constants (K') of 1. 4. lO 4 1/mole for methyl ,¢-D-mannopyranoside and o.3" IO 4 1/mole for methyl ~¢-D-...
متن کاملMonovalent derivatives of concanavalin A.
Monovalent dimers of concanavalin A (Con A) have been prepared by a combination of succinylation and photoaffinity labeling. Partial derivatization of native Con A using the photoaffinity label, p-azidophenyl-alpha-D-mannopyranoside, followed by affinity chromatography yielded a fraction that consisted of dimers with a single saccharide-binding site at pH 5. These monovalent dimers formed dival...
متن کاملEffect of concanavalin A dose, unbound concanavalin A, temperature, Ca2+ and Mg2+, and vinblastine on capping of concanavalin A receptors of human peripheral blood lymphocytes.
The capping of Concanavalin A (Con A) receptors induced by Con A was studied using human peripheral blood lymphocytes. The effects of Con A dose (5--100 micrograms/ml), pretreatment at 4 degrees C, unbound Con A, extracellular Ca2+ and Mg2+ and vinblastine were evaluated using Con A-horseradish peroxidase and electron microscopy. Lymphocytes incubated with Con A at 4 degrees C and fixed with gl...
متن کاملActivation of concanavalin A by Cd2+.
Binding of Cd2+ to concanavalin A and the subsequent induction of saccharide-binding activity has been studied at pH 6.5. We found that Cd2+ bound to both metal sites, S1 and S2, and that Cd2+ alone would induce sugar binding in concanavalin A. Using the fluorescent sugar 4-methylumbelliferyl alpha-D-mannopyranoside we determined that full saccharide-binding activity was obtained only when the ...
متن کاملConcanavalin a and Influenza Virus Infected Cells
Treatment of host cells with Concanavalin A prevents the assembly or release of fowl plague virus from chick fibroblasts and inhibits fusion of BHK cells by the paramyxovirus SV5. Metabolic events of the host cells are not greatly impaired during the early phase of infection. There is evi dence that the carbohydrate moiety of the Con A receptor of fowl plague virus is associated with the viral ...
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ژورنال
عنوان ژورنال: Nature
سال: 1977
ISSN: 0028-0836,1476-4687
DOI: 10.1038/265569b0