Sentence examples for mm were assayed from inspiring English sources

The chemical agents EDTA (10 mM) were assayed.

Four substrate concentrations in the range 0.5 mM - 2.5 mM were assayed to elucidate the mechanism of inhibition.

Once Mg2+ was identified as the optimal metal cofactor for PAP phosphatase activity, different concentrations of the metal ion (from 0 to 15 mM) were assayed in the presence of 100 µM PAP and 50 mM Tris buffer (pH 8.5).

Purified BRD4-1 (4 μM final concentration; 10 mM HEPES (pH7.5), 100 mM NaCl, and 1 mM DTT), and BRDT-1 (4 μM final concentration; 50 mM phosphate (pH7.4), 100 mM NaCl, and 1 mM DTT) were assayed, in quadruplicates, in a 96-well plate.

Comparative in vitro effects of everolimus and paclitaxel (10-5 M–10-12 M) after 24 hours on carotid endothelial (EC) and smooth muscle (SMC) cell viability under hyperglycemic (42 mM) conditions were assayed by ELISA.

In all cases, parallel reactions containing 4 mM potassium cyanide were assayed to confirm specific Complex IV activity.

Since this effect might depend on the compound level, different concentrations (in the range from 0.1 mM to 1 mM) of this carotenoid were assayed.

The effects of various metal ions and reagents on β-xylosidase activity were assayed at 10 mM and 20 mM concentrations (Figure 3B).

20S proteasome activities were determined similarly but using different reaction buffers: β1 and β2 activities were assayed in 25 mM HEPES, pH 7.5, 0.5 mM EDTA, 0.05% NP-40, 0.001% SDS.

Both BNO2 CGTase and Toruzyme were assayed in 10 mM sodium acetate buffer with 3 mM CaCl2 (pH 5.5).

Samples were assayed using 1 mM MUG (4-methylumbelliferyl-β-D-glucoronide) in extraction buffer followed by incubation of 2 3 hrs.