Sentence examples for km were calculated from inspiring English sources

All assays were performed in triplicate and repeated at least four times; Vmax and Km were calculated using Biosoft Kell Radlig software (Cambridge, UK).

Also, the Michael addition reaction rate constants (km) were calculated using microscopic acidic dissociation constant of ammonium groups in 4-aminobenzoic acid.

The Michaelis Menten kinetic model was found to fit satisfactorily for the hydrolysis of cod liver oil with both CCL and CRL enzymes and the kinetic parameters such as maximum rate of reaction (Vmax) and rate constant (KM) were calculated.

The kinetic aspects of DNA cleavage under pseudo- or true-Michaelis Menten conditrue-Michaelis Mentened, kineticonditionsrs (kcare KM) were calsolatedetailed3.57 h− 1, 6.92 × 10− 4 M; 0.28 h− 1, 1.9 × 10− 5 M for 4, respectively.

For long range propagation of a band-limited signal with frequencies from 100too 150 Hz in a North Pacific channel, signal waveforms, including arrival times and amplitudes at ranges from 44 to 4000 km, were calculated by using WKBZ and conventional normal mode (CNM) codes.

The maximum reaction velocity (Vmax) and Michaelis constants (Km) were calculated from Lineweaver-Burk plots (Lineweaver and Burk [1934]).

Strikingly, we found that the S111E phosphomimetic (kcat/ KM = 7.6 × 10 M−1s−1) but not a S111A mutant (kcat/ KM = 8.7 × 10 M−1s−1) led to a 13-fold decrease in GDP dissociation rate induced by Rabin8 compared to wild-type Rab8A (kcat/ KM = 1.0 × 10 M−1s−1) where the kcat/ KM is calculated by dividing the rate constant (kobs) of the reaction by the enzyme concentration (Fig 9B).

The apparent Michaelis Menten constant (Km) was calculated to be 0.45 ± 0.02 mmol L−1.

Its experimental detection limit was 0.7 μM (S/N = 3) and the apparent Michaelis Menten constant (Km) was calculated to be 18.35 mM.

The mass transport coefficient (km) was calculated based on pseudo-first order rate kinetics for both the electrode systems (graphite/graphite and SS304/graphite).

The Vmax of the bioconjugate, GOX, and Ox-GOX was estimated as 28.6, 6.2, and 6 IU μg−1 enzyme and the Km was calculated as 2.7, 9, and 9.5 mM, respectively.