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Three datasets were fit using a modified substrate inhibition equation with KM = Ki for identifiability and to prevent the Ki being less than KM.
The trial has entered its seventh week, with KM giving evidence in the past week.
b Interview with KM (November 2005).
The final weighted sum operation is accomplished with KM flops.
Activity was also demonstrated on xylobiose (X2), with Km 17.8 mM and Kcat 380 s−1.
In the present study, patients with NKM show significantly more plaque accumulation than patients with KM.
The enzyme catalyzes the cleavage and rejoining of oligonucleotide substrates in a sequence-dependent manner with Km = 42 microM and kcat = 2 min-1.
The specific activity of purified β-mannanase was 57.2 U/mg with Km and Vmax as 4 mg/ml and 63 µmol/ml/min, respectively.
The bacterially produced enzyme specifically converted borneol to camphor as the only product with Km and kcat values of 53 μM and 4.0 × 10−4 s−1, respectively.
Kinetic studies revealed that the mutant D103V L-ASNase has increased substrate affinity, with Km value of 0.42 mM and Vmax of 2778.9 μmol min−1.
Similar(1)
KM-HMR and KM-I2C are comparable in terms of execution time with KM-HMR performing better than the standard K-means algorithm and with KM-I2C generating better results than the KM-HMR algorithm.
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CEO of Professional Science Editing for Scientists @ prosciediting.com