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1 hastic character of inhibitor release, which obeys first-order kinetics.
2 us analyses of LpxH, we find HiLpxH does not obey surface dilution kinetics.
3 rfacial charge transfer is widely assumed to obey the Butler-Volmer kinetics.
4 te TcAPX activity indicating that the enzyme obeys Michaelis-Menten kinetics.
5 is proportional to enzyme concentration, and obeys Michaelis-Menten kinetics.
6 d neral, and with the E2 isozyme, only neral obeyed Michaelis-Menten kinetics.
7 haperone-mediated renaturation of luciferase obeyed Michaelis-Menten kinetics.
8 ual cells, transcription is a random process obeying single-molecule kinetics.
9 atch repair, has a slow ATPase activity that obeys Michalelis-Menten kinetics.
10 e nucleation events, and the transformations obey simple unimolecular kinetics.
11 rypsin, proteinase K, and thermolysin) while obeying Michaelis-Menten kinetics.
12 equilibrium was proven to be fully dynamic, obeying first-order equilibrium kinetics.
13 ble bond addition/electrocyclic ring opening obey saturation (Michaelis-Menten) kinetics.
14 80550 in normal liver (15.4 +/- 1.08 mL/min) obeyed first-order kinetics and did not vary over the do
15 naturation and aggregation of PKC because it obeyed pseudo-first order kinetics and because the hinge
16 corresponding T. brucei flavoprotein (TbALO) obeys Michaelis-Menten kinetics and can utilize both L-g
18 acceptor, hexaammineruthenium(III), does not obey ping-pong-pong kinetics, and alternative sites for
19 It exhibited both RT and RNase H activities, obeyed Michaelis-Menten kinetics, and was competitively
21 for T4 pol-DNA association and dissociation obeyed simple kinetics, at suboptimal Mg2+ concentration
22 from the sum of varying amounts of isoforms obeying Michaelis-Menten kinetics but with different val
23 sed to characterize interactions that do not obey pseudo-first-order kinetics due to the presence of
25 le level by fluorescence optical microscopy, obey the kinetics of stepwise polymerization, forming ch
26 ted protein (YAP) and Pin have been shown to obey single-exponential kinetics, the folding of the WW
28 me, the time dependence of product formation obeyed Michaelis-Menten-type kinetics throughout the ful
29 -dependent formation of glycosylated product obeys Michaelis-Menten-type kinetics throughout the cour
30 ysis of diaryl sulfate diesters was shown to obey first-order kinetics with respect to [(-)OH] and pr
31 wed that the most active antibody, MATT.F-1, obeyed classical Michaelis-Menten kinetics with a Km = 1
34 At pH 3.0, the reduction of LiPI by RNase obeys second-order kinetics with a rate constant of 4.7
35 he disappearance of both TPCPGa and DPMNCPGa obeys zero-order kinetics with rate constants (k) having
36 ding and dissociation kinetics were found to obey simple kinetics, with identical on rates (kon = 4.6
37 rylation of the substrate by PTPN1 and PTPN2 obeyed Michaelis-Menten kinetics, with KM values of 770
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