ライフサイエンスコーパス: inhibition constant

1 ent values for Km that depend on the product inhibition constant.

2 o inhibit the kinase activity with a similar inhibition constant.

3 r normally depends on prior knowledge of the inhibition constant.

4 polypeptides resulted in a decrease in each inhibition constant.

5 I(1)=0 and I(2)=E+K, where K is the apparent inhibition constant.

6 ro binding to the enzyme active site and for inhibition constants.

7 while inhibiting thrombin at low micromolar inhibition constants.

8 R2 = 0.89) between computed and experimental inhibition constants.

9 V, I47T, and S94A, have little impact on the inhibition constants.

10 ugh free energy simulations and experimental inhibition constants.

11 lysis of the temperature dependence of their inhibition constants.

12 bitors featuring label-free determination of inhibition constants.

13 , enzyme specificity constants, and apparent inhibition constants.

14 ons between SL3 RNA and NCp7 with micromolar inhibition constants.

15 he compounds possessed subnanomolar apparent inhibition constants.

16 inhibitor to ATP and OSB with low micromolar inhibition constants.

17 of inhibition by compounds with subnanomolar inhibition constants.

18 -ADAM displayed high affinity to SERT sites (inhibition constant = 0.081 nmol/L, using membrane prepa

19 tatin receptor subtype 2 with high affinity (inhibition constant, 0.13 +/- 0.03 nM).

20 it is not selective to a single OR subtype (inhibition constant, 0.4-1.6 nM across OR subtypes).

21 ed subnanomolar binding affinities for SERT (inhibition constants, 0.51 and 0.76 nM, respectively), h

22 ty similar to soluble fibrin fragment DD(E) (inhibition constant=0.53-0.83 muM).

23 A potent (inhibition constant = 37 picomolar) neuronal nicotinic a

24 e.g. XK216, the least potent inhibitor (Ki (inhibition constant) = 4.70 nM), possesses the smallest

25 ase and phosphatase activities with the same inhibition constant; a point mutation that weakens phosp

26 at both the P2 and P2' positions and has an inhibition constant against plasmin of 5 microM.

27 The inhibition constants against papain of the CysPIs encode

28 Fab A11 was identified with a 720 pM inhibition constant and high specificity for matriptase

29 deviation of 0.8 log Ki units from measured inhibition constants and an R2 value of 0.74.

30 on of a known inhibitor of shikimate kinase; inhibition constants and mode of inhibition were accurat

31 ytes, a clear correlation between the enzyme inhibition constants and P. falciparum inhibition concen

32 strong correlation was observed between the inhibition constants and the biosensor sensitivity.

33 s curves and yields estimates of the in vivo inhibition constants and the rate constants for eliminat

34 Evaluation of the inhibition constants and the rates at which both the alp

35 ("true") values of the uninhibited velocity, inhibition constant, and total enzyme concentration were

36 num inhibit blood coagulation with picomolar inhibition constants, and have been targeted as novel ph

37 ic properties (steady and pre-steady state), inhibition constants, and thermodynamic properties of E:

38 rresponds to the rate of inhibition, and the inhibition constants are in the micromolar range but var

39 is disrupted, enzyme kinetic parameters and inhibition constants are similar to those obtained for s

40 Pmf-containing inhibitors show inhibition constants as low as 8 nM in extracellular Grb

41 y effective at inhibiting the protease, with inhibition constants as strong as 40 nM.

42 thod with respect to the detectable range of inhibition constants (both classical and tight-binding)

43 both human and mouse FAP with low nanomolar inhibition constants but does not inhibit close FAP homo

44 lass, CM026 and CM037, exhibit submicromolar inhibition constants but have different mechanisms of in

45 Determination of tight-binding inhibition constants by nonlinear least-squares regressi

46 The inhibition constant calculated from these parameters (Ki

47 However, the inhibition constant calculated was dependent on the conc

48 The inhibition constants calculated from the slow-binding in

49 ive site concentration and the tight-binding inhibition constant can be determined simultaneously fro

50 ) and of (55)Fe(2+) transport by Mn(2+) gave inhibition constants comparable to each cation's K(a) fo

51 correlate with their Michaelis constants or inhibition constants, consistent with their exerting an

52 omplexation was very similar to the relative inhibition constant derived from solution phase kinetics

53 rocedure for the estimation of tight-binding inhibition constants directly from dose-response data.

54 involved in this 150-fold difference in the inhibition constant for 2164U90.

55 The inhibition constant for amiloride was 1 microM at 0.013

56 (2) The inhibition constant for Ca2+ dissociation from this site

57 The inhibition constant for EAEIFEAIE, a competitive inhibit

58 inhibitor (TFPI) that critically reduces the inhibition constant for FXa to below the plasma concentr

59 The K(i) inhibition constant for PY957 showed greatest potency of

60 sm correctly predicts the observed change in inhibition constant for the complex of A77003 and the re

61 o disrupt enzyme-inhibitor interactions, and inhibition constants for 13 inhibitors were determined t

62 ation efficiency of 2a and 3a as well as the inhibition constants for 1a, 4a, and 5a.

63 In this article, we present inhibition constants for 21 compounds, including a serie

64 pable of easily measuring kinetic values and inhibition constants for a range of natural and nonnatur

65 ared to CA II (6.2 vs 6.9), as well as lower inhibition constants for a variety of anions, including

66 Here we report crystal structures and inhibition constants for bulkier dipeptide inhibitors bo

67 pH dependencies of the inhibition constants for competitive inhibitors identifi

68 say, we examined the correlation between the inhibition constants for enzyme activity (Ki values) and

69 most potent compounds display sub-nanomolar inhibition constants for factor Xa and show greater than

70 The substrates were used to obtain inhibition constants for four inhibitors that are common

71 most potent compounds (33, 35, and 37) have inhibition constants for human FXa of 3.9, 2.3, and 0.83

72 Inhibitors which provide nanomolar inhibition constants for IU-nucleoside hydrolase exhibit

73 s of thioxolone yielded similar estimates of inhibition constants for most compounds, although two co

74 Designed peptides showed low-micromolar inhibition constants for N2P2 and no detectable M3P6 bin

75 Apparent inhibition constants for novobiocin increased linearly w

76 The effects of pH on the inhibition constants for pepstatin A and the substituted

77 nication so that the apparent activation and inhibition constants for regulators depended upon each o

78 RYM1 showed nanomolar range inhibition constants for several MMPs.

79 uring the SKIE on the noncompetitive (mixed) inhibition constants for the C-terminal reaction product

80 re, and we suggest that the magnitude of the inhibition constants for the dead-end inhibitors may pro

81 r IU-nucleoside hydrolase exhibit micromolar inhibition constants for the IAG-enzyme.

82 In contrast, the inhibition constants for the propeptides of prothrombin

83 The best-fit value of the apparent inhibition constants for the tight-binding inhibitor was

84 ethers, respectively) were the best, and the inhibition constants for the two were comparable.

85 onship between these two enzymes and similar inhibition constants for these two enzymes with several

86 tyrosine phosphatase 1B with low micromolar inhibition constant, high selectivity (30-fold) over the

87 The inhibition constants, IC(50), K(I) values, and inhibitio

88 This method was also used to determine the inhibition constant (IC50 value) for the competitive inh

89 200 microM NMDA-evoked responses with a 50% inhibition constant (IC50) of approximately 1 microM at

90 e from Arabidopsis thaliana (GST-rAtKS) with inhibition constants (IC50 = 1 x 10-7 and 1 x 10-6 M) si

91 The inhibition constants (IC50) were 0.70, 1.46, 6.28, 10.4,

92 e DELI tended to produce higher half-maximal inhibition constants (IC50s) than FCM, with an overall b

93 e, produced an 8-fold increase in the enzyme inhibition constant in contrast with the abolition of ca

94 PEP and OAA in order to achieve a micromolar inhibition constant in the absence of direct coordinatio

95 ibitor of its parent enzyme, with an overall inhibition constant in the low nanomolar range.

96 of hits by rapid and accurate measurement of inhibition constants in continuous assays, and pre-stead

97 utants resemble those of PR(WT) with similar inhibition constants in good agreement with the antivira

98 three of the phosphate inhibitors displayed inhibition constants in the 4-5 nM range, indicating tha

99 osaccharomyces pombe lumazine synthase, with inhibition constants in the low nanomolar to subnanomola

100 ncompetitive or linear mixed inhibitors with inhibition constants in the millimolar concentration ran

101 prisingly all potent HNMT inhibitors, having inhibition constants in the range of 10-100nM.

102 o the development of potent antibiotics with inhibition constants in the single-digit picomolar range

103 d sensitive to adefovir diphosphate with the inhibition constant increased by only 2.3-fold.

104 d sensitive to adefovir diphosphate with the inhibition constants increasing by 1.3-fold and 2.2-fold

105 alogues were further analyzed for their P-gp inhibition constant, intrinsic toxicity, and potency to

106 By assuming that the inhibition constant is independent of temperature over t

107 he hydration constant for AcLF-13CHO and its inhibition constant, its K(d) is 16 microM, 8000-fold la

108 iol group, resulting in an inhibitor with an inhibition constant K(i) = 40 nM.

109 ashed PSII (1.5-5 mM), whereas values of the inhibition constant K(I) in intact PSII (9-17 mM) were l

110 enzyme in a fast equilibrium, defined by the inhibition constant K(i), to form an initial reversible

111 olecular tongs to date were obtained with an inhibition constant K(id) of 50 nM for PR and 80 nM for

112 protocol for the rapid determination of the inhibition constant ( K (i)) for competitive inhibitors

113 ioligand for competition studies to evaluate inhibition constants ( K i).

114 site in our model, significantly affect the inhibition constant (K i) of P-CABs.

115 itor in this series (72, SE170) has a potent inhibition constant (K(i) = 0.3 nM), is 350-fold selecti

116 inorganic phosphate (P(i)) in excess of its inhibition constant (K(i) approximately 1 muM).

117 a series of quinuclidine derivatives with an inhibition constant (K(i)) < 6 nmol/L (33 pmol/L for 4)

118 g activity on G4 DNA but not duplex DNA: the inhibition constant (K(i)) for NMM inhibition of G4 DNA

119 The BLIP inhibition constant (K(i)) for PC1 beta-lactamase was me

120 d into the PAP active site with a calculated inhibition constant (K(i)) more favorable than that of t

121 phthaloyl-L- ornithine] was found to have an inhibition constant (K(i)) of 0.35 +/- 0.10 pM against h

122 lyses were active and inhibited YprA with an inhibition constant (K(i)) of 1.7 nM, and the addition o

123 is a slow-binding inhibitor with an overall inhibition constant (K(i)) of 2 nM and a dissociation ra

124 ] cluster to an apo-acceptor protein with an inhibition constant (K(i)) of 200 mum, which reflects th

125 as obtained, which binds to Bcl-x(L) with an inhibition constant (K(i)) of 36 +/- 2 nM.

126 The inhibition constant (K(i)) of isozyme-selective PDE inhi

127 Kinetic analysis of the inhibition constant (K(i)) of MMP-8 (K(i) = 36 microM) a

128 Additionally, the overall inhibition constant (K(i)) of oxypurinol for HS6B-XO was

129 ivity was Na(+) sensitive with a significant inhibition constant (K(i)) shift observed following K(+)

130 dinium iodide (11), which had an equilibrium inhibition constant (K(i)) value of 219 nM at human A(3)

131 The inhibition constant (K(i)) values calculated from these

132 PKM-zeta, PKC-iota and PKC-zeta with similar inhibition constant (K(i)) values.

133 alf-maximal inhibitory concentration (IC50), inhibition constant (K(i)), and the inhibition mechanism

134 g competitive component [i.e., a competitive inhibition constant (K(ic)) of 0.12 +/- 0.02 mM and an u

135 c)) of 0.12 +/- 0.02 mM and an uncompetitive inhibition constant (K(iu)) of 3.04 +/- 0.74 mM].

136 xhibited strong inhibition, with equilibrium inhibition constants (K(i) values) from 0.38 to 1.7 micr

137 By comparing inhibition constants (K(i) values), inhibitor solubiliti

138 inhibition by triclosan, with uncompetitive inhibition constants (K(i)') of 0.18+/-0.01 and 0.12+/-

139 -1) protease (enzyme, E) that values for the inhibition constants (K(i)) could not be determined by c

140 fy the mechanism of inhibition and determine inhibition constants (K(i)) for a weak competitive inhib

141 To demonstrate this principle, inhibition constants (K(I)) for selected acrylates rangi

142 riments with [(3)H]adenosine, P2 transporter inhibition constants (K(i)) have been determined for a d

143 cosine and dansyl-L-asparagine from HSA with inhibition constants (K(i)) of 85 +/- 3 microM and 1500

144 The inhibition constants (K(i)) of E,E-5, E,Z-5, Z,E-5, and

145 c resistance to famciclovir, we compared the inhibition constants (K(i)) of penciclovir triphosphate

146 inases (TIMPs), we have assessed equilibrium inhibition constants (K(i)) of putative physiological in

147 Inhibition constants (K(i)) of the antiviral drug indina

148 The inhibition constants (K(i)) of TMC-114 for mutants PR(D3

149 Inhibition constants (K(i)) range from 2 to 250 nM for t

150 noesterase activity of lambdaPP, albeit with inhibition constants (K(i)) that range over 5 orders of

151 that association rate constants (k(on)) and inhibition constants (K(i)) were similar to those for ot

152 ues, as demonstrated by 13- and 6-fold lower inhibition constants (K(i)), respectively.

153 riphosphate was assessed by determination of inhibition constants (K(i)).

154 eceptor with tritiated spiperone to evaluate inhibition constants (K(i)).

155 ceptors with tritiated spiperone to evaluate inhibition constants (K(i)).

156 ition models were used to determine apparent inhibition constants (K(I)*) for the inhibitors.

157 icin tetraloop gave slow-onset tight-binding inhibition constants (K(i)*) of 2.3-8.7 nM under physiol

158 trated picomolar affinity at D(2)RHigh (mean inhibition constant [K(i)] = 85 pM) and excellent select

159 The pH dependence of the competitive inhibition constant, K(i), for CdBcII with l-captopril i

160 n acceptors, although the value of the slope inhibition constant, K(is), was 25-30-fold greater with

161 The effective steady-state inhibition constants, K(i), are nanomolar, e.g., 0.11 nM

162 r solution over the range 0-9% increases the inhibition constants, K(i), by up to an order of magnitu

163 mbinant delta-dendrotoxin has a half-maximal inhibition constant (Kd) of 150 nM when applied to ROMK1

164 ically determining the apparent dissociation-inhibition constant (Kdi) for the inhibitors.

165 farnesyl transferase inhibitor (FTI) with an inhibition constant Ki = 3.0 nM.

166 pecifically inhibited by triacsin C with the inhibition constant Ki in the nanomolar range.

167 dard error of the mean (SEM), n = 16) and an inhibition constant Ki of 0.59 mM +/- 0.07 (mean +/- SEM

168 e well correlated with literature values for inhibition constants Ki and kcat/Km for the correspondin

169 tations in its interface, that has an MMP-14 inhibition constant (Ki ) of 0.9 pm, the strongest MMP-1

170 -Cbl) displaces E-peptide-1 with a nanomolar inhibition constant (Ki = 78.9 +/- 5.6 nm).

171 For the viral enzyme the logarithm of the inhibition constant (Ki) correlated with neither the log

172 he enzymatic activity of scuPA/suPAR with an inhibition constant (Ki) equal to 1.9 microM, increased

173 ), k(cat), and k(cat)/K(m)) and the apparent inhibition constant (Ki) for adenosine 5'-diphosphate (A

174 e second-order rate constant (ki/Ki) and the inhibition constant (Ki) for inhibition of human alpha-t

175 In both cases, the kinetic inhibition constant (Ki) is 25 +/- 10 microM.

176 functional assays in rabbit vas deferens and inhibition constant (Ki) of 0.02 nM measured in radiolig

177 inhibited by fluoride ion at pH 8.0 with an inhibition constant (Ki) of 30 mM.

178 -350 nM, in good agreement with the in vitro inhibition constant (Ki) of 6.3 nM and regional Bmax in

179 fected cells is inhibited by lipoate with an inhibition constant (Ki) of approximately 5 microM.

180 rely competitive manner, with an equilibrium inhibition constant (Ki) of less than 3.8 nM.

181 efficiency were used in conjunction with the inhibition constant (Ki) to evaluate the advantage of th

182 atechuate is a competitive inhibitor and the inhibition constant (Ki) was obtained as 0.23 muM but do

183 However, the inhibition constant (Ki), and therefore also the second-

184 In this manner, the value of the microtubule inhibition constant (Ki), which is the binding constant

185 he previously noted correlations between the inhibition constants (Ki 170-1.2 microM) and the chemica

186 valid for the calculation of the competitive inhibition constants (Ki values) for inhibitors in the F

187 The inhibition constants (Ki) are in the 10(-7)-10(-9) M ran

188 The apparent inhibition constants (Ki) for BIR2-mediated inhibition o

189 to change Asp-49 and Phe-142 to alanine, and inhibition constants (Ki) for both mutants were determin

190 en constant (Km) for 3beta-HSD substrate and inhibition constants (Ki) for epostane and trilostane to

191 Inhibition constants (Ki) for the double mutant K47Q;D48

192 ent monoglutamate against DHFR (7.0 nM), the inhibition constants (Ki) for the parent monoglutamate a

193 d resistance to lamivudine triphosphate with inhibition constants (Ki) increased by 8.0-fold, 19.6-fo

194 amin K-dependent proteins by determining the inhibition constants (Ki) toward a factor IX propeptide/

195 ceptors with tritiated spiperone to evaluate inhibition constants (Ki).

196 idylprolyl isomerase activity of FKBP12 with inhibition constants (Ki,app) approaching 0.10 microM.

197 , we identified 30 potential lead compounds (inhibition constant, Ki= 1-32 microM) representing nine

198 The steady-state inhibition constants, Ki, for 7d and 7n were calculated

199 Values of inhibition constants, Ki, for a family of structurally r

200 The values of the inhibition constants, Ki, were the following: Ac-R-R-K-W

201 rmed experimentally by measuring competitive inhibition constants KI2 for propidium and tacrine, inhi

202 howing how the variation in apparent product inhibition constants (Kii) can be used to predict the ra

203 tion by thioacetyl-lysine peptide yielded an inhibition constant (Kis) of 0.017 microM, 280-fold lowe

204 with acetyl-lysine substrate and yielded an inhibition constant (Kis) of 4.8 microM, similar to its

205 Normally an initial estimate of the inhibition constant must be provided by the investigator

206 nversely, the determination of tight-binding inhibition constants normally requires prior knowledge o

207 potent inhibitor 8 binds to plasmin with an inhibition constant of 0.2 nM, whereas K(i) values >1 mu

208 ting divalent inhibitor exhibits an in vitro inhibition constant of 165 pM against the BoNT/A catalyt

209 binding affinity of nifrolidine exhibited an inhibition constant of 2.89 nmol/L for the alpha(4)beta(

210 is a potent inhibitor of factor XIa with an inhibition constant of 250-400 pM.

211 catalytic/disintegrin domain with an overall inhibition constant of 280 +/- 34 nM and high specificit

212 bited by a recombinant Kunitz domain with an inhibition constant of 344 +/- 37 pM versus 422 +/- 33 p

213 a-1-fucose (GDP-2F-Fuc) was observed with an inhibition constant of 4.2 microM which represents the m

214 Ia is inhibited by protease nexin II with an inhibition constant of 437 +/- 62 pM, compared to 229 +/

215 proteolytic active site to yield an overall inhibition constant of 5-20 nM.

216 xed-type inhibitor of Gsp synthetase with an inhibition constant of 6 microM for the inhibitor bindin

217 When an acetate product inhibition constant of 600+/-31M(-1), determined by isot

218 ecombinant human IDO (rIDO) with an apparent inhibition constant of 94 +/- 17 nM.

219 uggest L-lysine binds to free enzyme with an inhibition constant of about 5 mM.

220 The most potent analog (with an inhibition constant of about 50 nM) displayed a minimal

221 ducing its binding affinity with an apparent inhibition constant of approximately 0.2 mM.

222 t-induced activation of the receptor with an inhibition constant of approximately 150 microM.

223 petitive inhibition versus cysteine, with an inhibition constant of approximately 306 nM versus ATP.

224 everely impaired carboxylase binding with an inhibition constant of at least 200,000-fold weaker than

225 These findings were corroborated when the inhibition constant of binding to Bcl-XL was determined

226 ssociation constant of (3)H-prazosin and the inhibition constant of CUMI-101.

227 hammerhead by approximately 15-fold with an inhibition constant of K(i) = 30.9 +/- 2.3 microM.

228 ively) were 500 to 1000 times lower than the inhibition constant of L1 (19,000 nM).

229 s (IC(50) = 2.4 nM) correlated well with the inhibition constant of MII[H9A;L15A] for [(125)I]alpha-c

230 a two-carbon linker led to a decrease of the inhibition constant of the resulting compound by 3 order

231 und to be competitive inhibitors of AAP with inhibition constants of 0.24 and 4.6 mM, respectively.

232 Compound 1 had inhibition constants of 17-fold, 8-fold, 3-fold, and 3-f

233 hibition of transport on mOat3 in cells with inhibition constants of 198 +/- 39, 558 +/- 75, 745 +/-

234 variable substrate with apparent competitive inhibition constants of 2.1, 36, and 29 microM, respecti

235 GRL-5010A and GRL-4410A show inhibition constants of 4.3 +/- 7.0 and 1.7 +/- 1.8 nM,

236 0 A, respectively, and measured the apparent inhibition constants of 5G9 on a panel of TF mutants.

237 udine-resistant hepatitis B virus (HBV), the inhibition constants of adefovir diphosphate and lamivud

238 two descriptors explained 90% of variance in inhibition constants of all 28 inhibitors, ranging from

239 as used for measuring binding affinities and inhibition constants of BACH1 peptides and small molecul

240 Moreover, the inhibition constants of moenomycin and two previously id

241 a DDAH-1 selective inhibitor, as seen in the inhibition constants of N5-(1-iminoethyl)-, N5-(1-iminop

242 device was used for the MS determination of inhibition constants of several inhibitors of HIV-1 prot

243 Inhibition constants of the aptamers were determined and

244 comparison with the nucleoside derivatives, inhibition constants of their corresponding 5'-phosphory

245 The inhibition constants of these compounds toward five diff

246 avir, and reduced dimer stability, while the inhibition constants of two peptide analog inhibitors we

247 h a Ki of 24 microM and a Ki* (isomerization inhibition constant) of 0.88 microM.

248 using equilibrium dialysis and to the K(i) (inhibition constant) of 6.7 microm for CoA obtained from

249 ncubation interval significantly affects the inhibition constants on a structurally dependent basis.

250 rgets, pairs that have binding affinities or inhibition constants ranging from subnanomolar to low mi

251 ues: TdF or TdCD, and also consistent enzyme inhibition constants reported in the literature.

252 presence of Ca(2+) with a stoichiometry and inhibition constant similar to those for the binding to

253 luco- and galacto-configured inhibitors, the inhibition constants suggested preferred recognition of

254 Furthermore, the similarity of amiloride inhibition constants suggested that the channel in neona

255 , normal SKIE values were observed for these inhibition constants, suggesting that both kinetic and t

256 s to members of the RNase A superfamily with inhibition constants that span 10 orders of magnitude.

257 losed conformer seen with DEER and enzymatic inhibition constants, thermodynamic dissociation constan

258 sing clustering of experimentally determined inhibition constants (to define specificity classes of k

259 In contrast to studies with AAC(6')-Ii, the inhibition constants toward AAC(6')-Iy are essentially i

260 The compound has an inhibition constant value of 80 pM, and demonstrates 37

261 racer with high affinity for aggregated tau (inhibition constant value, 8 nM) and high (>/=500x) in v

262 ts with a relatively wide range of estimated inhibition constant values (K(i) values = 169-1147 micro

263 Statins are HMGR inhibitors with inhibition constant values in the nanomolar range that e

264 The apparent inhibition constant values of foscarnet against mutant U

265 The most potent, compound 3, had a picomolar inhibition constant versus BChE due to strong cation-pi

266 Its equilibrium inhibition constant was calculated to be < 20 nM.

267 P,4-P), having the most favorable calculated inhibition constant, was synthesized and characterized.

268 Inhibition constants were calculated from the level of e

269 Inhibition constants were determined for over half of th

270 ed by tert-butyl hydroperoxide, and apparent inhibition constants were determined to be between 33 an

271 s were used in preparing (86)Y- 4: - 6: PSMA inhibition constants were evaluated by competitive bindi

272 an EIS or ESI complex formed, the respective inhibition constants were far lower than K(ss).

273 The inhibition constants were generally similar for all HDAC

274 Even with inhibition constant, when inhibitory synchrony was highe

275 Both assays gave similar inhibition constants with a known tyrosine kinase inhibi

276 was examined in more detail by measuring the inhibition constants with Torpedo AChE, fetal bovine ser