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The binding capacity of each polymer in the library was analyzed in two different solvents.
Isotherm studies were utilized to determine the binding capacity of each of the nanomaterials for Cu2 + and Pb2 +.
The relative binding capacity of each divalent metal was greatly affected by the presence of other divalent metals.
The binding capacity of each metal decreased, under competitive binding conditions (with a range of metal ions present at 17.8 μN), to 1.3 and 0.17 μmol cm−2, respectively, indicating stronger selectivity for Cu2+.
GO@MPBA exhibited the high binding capacity towards glycoproteins such as ovalbumin (1288.8 mg g−1), immunoglobulin G (1144.1 mg g−1), transferrin (592.1 mg g−1) and horseradish peroxidase (392.4 mg g−1), in contrast, the binding capacity of each non-glycoproteins (cytochrome c, deoxyribonuclease A, pepsin, trypsin, lysozyme and bovine serum albumin) is less than 50 mg g−1.
Having established the specificity of the interaction between GFP-L22 and SL3, we next tested the RNA binding capacity of each mutated L22 protein.
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These bispecific antibody fragments not only retained the antigen-binding capacity of each of the parent antibodies, but also are capable of binding to both targets simultaneously as demonstrated by a cross-linking ELISA.
Next we correlated the effects of trastuzumab and T-DM1 to the trastuzumab-binding capacity of each cell line [ 40].
These data show that the phosphorylation of LAT is not substantially different among the cell lines, indicating the binding capacity of LAT in each cell is similar.
To address available site II–specific binding capacity of albumin before and after each ECAD cycle, albumin-binding capacity (ABiC) was measured in plasma samples as previously described [ 18].
A mixture of a purified candidate biotin derivative and its reference ligand (BMPL or BPDEDA) at equal molar quantities was added to Tris-HCl buffer in 2.0 mL containing 400 μL SMPP for the total binding capacity of over 1.6 nmol, and each biotin derivative of interest had the final level of 0.2 μM.
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