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1 ubstrates, whereas AP3 hydrolyzed only L-Arg-beta-naphthylamide.
2 Only AP2 hydrolyzed L-Val-beta-naphthylamide.
3 ne 6G, ciprofloxacin, nafcillin, and Phe-Arg-beta-naphthylamide.
4 s cleaved collagen analogs Gly-Pro 4-methoxy-beta-naphthylamide, 2-furanacryloyl-Leu-Gly-Pro-Ala (FAL
5 -Leu-beta-naphthylamide and 25% of the L-Arg-beta-naphthylamide activities were localized in the chlo
6 ities of the enzyme and substrate, L-leucine beta-naphthylamide, allowed for efficient mixing in an o
9 AP3 were the only ones reacting against Val-beta-naphthylamide and Arg-beta-naphthylamide, respectiv
10 he cleavage of trypsinogen or Gly-(Asp)4-Lys-beta-naphthylamide and reduced the rate of inhibition by
11 -state kinetic parameters for both aminoacyl-beta-naphthylamide and unmodified dipeptide substrates o
12 AbetaN homologs, Ala beta-naphthylamide, Arg beta-naphthylamide, and Phe beta-naphthylamide, as subst
13 amined the behavior of PAbetaN homologs, Ala beta-naphthylamide, Arg beta-naphthylamide, and Phe beta
14 phthylamide, Arg beta-naphthylamide, and Phe beta-naphthylamide, as substrates of AcrB and as modulat
16 ptibility testing in the presence of Phe-Arg-beta-naphthylamide dihydrochloride and 1-(1-naphthylmeth
21 g azithromycin MICs (with or without Phe-Arg-beta-naphthylamide [PAbetaN], an efflux inhibitor), [(14
22 ylene blue or MacConkey agar, L-pyrrolidonyl-beta-naphthylamide (PYR), and 4-methylumbelliferyl-beta-
23 phthylamide-labeled substrate L-pyrrolidonyl-beta-naphthylamide (PYR), the nitrophenyl-labeled substr
24 cting against Val-beta-naphthylamide and Arg-beta-naphthylamide, respectively, several protease inhib
25 ly hydrolyzes amino acid-p-nitroanilide and -beta-naphthylamide substrates with N-terminal Leu, Met a
26 inhibition of auxin transport by artificial beta-naphthylamide substrates, and saturable displacemen
29 synthetic substrate Gly-Asp-Asp-Asp-Asp-Lys-beta-naphthylamide was cleaved with similar kinetic para
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