Sentence examples for enzyme stock from inspiring English sources

A 20 µL of acarbose or test compounds solution was incubated for 7 min with 150 µL of enzyme stock at 37 °C.

The inhibition was measured spectrophotometrically at pH 7.0 and 37 °C employing 2 mM p-nitrophenyl α-d-glucopyranoside (PNP-G) as a substrate and 32 mU/mL of enzyme, in 100 mM potassium phosphate buffer (enzyme stock).

Examinations with tyrosinase (PPO) were equally performed in sodium phosphate buffer (NaPP, 100 mM, pH 6.5) containing 20 μL of a enzyme stock solution (1 mg lyophilized powder dissolved in 1 mL NaPP, with an activity of ≥1000 U mg-1), with monitoring enzyme activity after addition of 5 mM catechol (final concentration, λ = 450 nm) at 25°C.

Enzyme stock concentrations and specific activities are the same as previously reported [20].

The effect of trypsin on the formation of serum-derived NLP was studied by adding this enzyme (stock solution of 5% in DMEM, pH 7.4) to a final concentration of 0.5% in serum-containing DMEM, followed by incubation at 37°C for 2 hours prior to the addition of NLP precipitating reagents.

Enzyme stock solutions were stored at −80 °C until use.

Two enzyme stocks of different purities were used but total phenols removal was independent of enzyme purity.

Concentrated enzyme stocks were diluted into assay buffer in siliconized Eppendorf tubes to reach concentrations of 1 4.6 μM for all proteases, with final concentrations determined by a Hewlett-Packard 8453 UV vis spectrometer (1 cm path length).

Before use, FL APE1 enzyme stocks were diluted in a buffer containing 50 mM HEPES (pH 7.5), 50 mM KCl, 1 mM MgCl2, and 1 mM DTT to a concentration 2-fold higher than the final value.

Once cooled, 40 μl of buffer-enzyme stock was added.

The buffer-enzyme stock consisted of 8% CTec2 (Novozymes) in 1 M sodium citrate buffer.