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One unit of enzyme activity was defined as the amount of enzyme that catalyzed the release of 1.0 μmol CoA/min using a molar absorption coefficient of 13,600 M−13,600.
Carbonyl content was determined spectrophotometrically at 370 nm using a molar absorption coefficient of 22,000 M−1 cm−1 [18].
The peptide concentration was calculated from the absorbance at 280 nm using a molar absorption coefficient ε280 of 6,970 M−1cm−1.
Carbonyl content was determined spectrophotometrically at 370 nm using a molar absorption coefficient of 22,000 M−1cm−1 [27] [27].
Peptide concentrations were determined using a molar absorption coefficient at 280 nm equal to 1 280 M−1 cm−1 for the tyrosine-containing peptides α4, INH5 and HTHi and 5600 M−1 cm−1 for the tryptophane-containing peptides K156 and wt IN.
The carbonyl content was calculated using a molar absorption coefficient of 22,000/M-cm = ɛ.
Similar(48)
Protein concentrations were determined from the absorbance at 280 nm using a molar absorptivity constant of each protein.
Protein concentrations were determined from the absorbance at 280 nm using a molar absorptivity constant (ε280 = 103,280 M−103,280.
The concentration of Dylight549 bound to the ocr dimer was calculated from absorption using a molar extinction coefficient of 150 000 M−1 cm−1 at 562 nm.
Bis-ANS concentration was determined using a molar extinction coefficient of 16,790 M−1 cm−1 at 385 nm51.
Calculations were made using a molar extinction coefficient of 9.6 mM−1 cm−1.
More suggestions(15)
using a commercial absorption
using a continuous absorption
using a solvent absorption
using a volumetric absorption
using a total absorption
using a Atomic absorption
using a dynamic absorption
using a molar ratio
using a molar extinction
using a atomic absorption
using a A-band absorption
using a simple absorption
using a molar coefficient
using a molar concentration
using a molar vector
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