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1 ty acids, yielding the highest activity with p-nitrophenyl acetate.
2 its esterase activity and ability to cleave p-nitrophenyl acetate.
3 thin the first 5 min of reaction with 0.5 mm p-nitrophenyl acetate.
4 identify residues that become acetylated by p-nitrophenyl acetate and determine the relationship bet
5 terase activity was confirmed in vitro using p-nitrophenyl acetate and O-acetylated PG as substrates.
6 rasts with reactions of aryl oxide ions with p-nitrophenyl acetate and with similar acyl transfers wh
7 -natural substrates, such as phenyl acetate, p-nitrophenyl acetate, and the organophospate paraoxon.
8 istidine-mediated nucleophilic hydrolysis of p-nitrophenyl acetate as a model reaction, and the ORBIT
9 , namely, the pre-steady-state hydrolysis of p-nitrophenyl acetate by the enzyme chymotrypsin, the ki
12 d-free human albumin was treated with 0.5 mm p-nitrophenyl acetate for 5 min to 2 weeks, or with 10 m
14 ng enzyme kinetics, the standard reaction of p-nitrophenyl acetate hydrolysis by chymotrypsin was ana
15 ted position, while catalytic efficiency for p-nitrophenyl acetate hydrolysis can be retained regardl
16 ombinant PelA hydrolyzed the pseudosubstrate p-nitrophenyl acetate in vitro, and site-specific mutati
17 state and steady state kinetic analysis with p-nitrophenyl acetate (PNPA) and NAT2 revealed a single-
19 acetyl donors, acetyl coenzyme A (AcCoA) and p-nitrophenyl acetate (PNPA), and four arylamine substra
20 me, and increased hydrolytic activity toward p-nitrophenyl acetate (pNPA), the substrate used for evo
22 f NAD(H) increased the rate of hydrolysis of p-nitrophenyl acetate showing that the metal only affect
24 When a more sensitive esterase substrate, p-nitrophenyl acetate was utilized, only 21.4% and 0.6%
25 utamic acid triads on each helix, hydrolyses p-nitrophenyl acetate with catalytic efficiencies that m
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