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At the concentrations tested, the recognition process occurs between tubulin and the immobilized GEC1; moreover enhanced binding was obtained with the home-made 2D sensing layer more than with 3D carboxymethyl dextran matrix.
A dose-dependent reduction of the CS6-mediated sulfatide binding was obtained with the highly sulfated polymer dextran sulfate, but not with dextran, demonstrating the importance of the sulfate group for binding to occur.
When using recombinantly expressed and purified CssA and CssB subunits of the CS6 complex, sulfatide binding was obtained with the CssB subunit, demonstrating that the glycosphingolipid binding capacity of CS6 resides within this subunit.
The optimal binding was obtained with a (GlcNAc 5.
The highest antibody binding was obtained with MorHap-BSA conjugates containing 3 5 haptens.
By contrast, an 87% mean inhibition (range 80 92%) of patients IgE binding was obtained with polyclonal Phl p 5-specific IgG antibodies (Table 3).
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The (4S -FPro turned out to be a DNA binder with lower specificity; comparable binding was obtained for 3,4S -FProoproline witurnedlanar ring coutormatoon.
With regard to the (α4 2 β2)3-TMD sthechiometry, the docking results indicate that the most favorable energy of binding was obtained for (S --mecamylamine interacting with L1 (Table 1), which iS --mecamylamine cytoplaS --mecamylaminee interacting.
Non-specific binding was obtained from two competitive homologous binding assays with non-radioactive Ga68-PSMA-11.
Specific binding was obtained by subtracting non-specific binding from total binding.
The lowest binding constant was obtained with phenylbutazone as site probe suggesting site I (sub-domain IIA) as the principal binding site for rivaroxaban (Fig. 3d).
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