Sentence examples similar to binding capacities of each from inspiring English sources

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.

After appropriate calibration of the fluorescence signals, we estimated the binding capacity of each bead population, which ranged from 0 to ∼200,000 molecules of biotin-PE.

First we analyzed the binding capacity of each purified scFv to the E7 protein covalently coupled to a CM5 sensor chip.

Despite the extremely tight streptavidin-biotin interaction, only about 15 – 40% of viral particles were bound to the surface of streptavidin-coated wells under the conditions used where the number of viral particles applied was considerably below saturation of the well surface (estimated by both dimensional and biotin-binding capacities of each well).

The binding capacities of the particles were evaluated by equilibrium binding experiments.

Maximum binding capacities of 45.23, 44.83 and 42.44 mg g−1 for RMN, ATMN and BTMN, respectively, were obtained.