ライフサイエンスコーパス: Menten

1 us polarimetric assay) enabled Michaelis and Menten to establish the existence of a quantitative rela

2 Michaelis and Menten's classic 1913 paper on enzyme kinetics is used t

3 erved as the cornerstones for Michaelis' and Menten's seminal 1913 paper.

4 aken in 1913, when Leonor Michaelis and Maud Menten published their studies of sucrose hydrolysis by

5 Michaelis-Menten analysis demonstrates that the kinetic enhancemen

6 Michaelis-Menten analysis revealed that the ATPase has a k(cat) of

7 Michaelis-Menten apparent constant, KM(app), was determined as 0.3

8 Michaelis-Menten enzyme kinetic studies provide mechanistic detail

9 Michaelis-Menten experiments showed that Ric-8BFL elevated the V(m

10 Michaelis-Menten kinetic parameters from amino acid activation ass

11 Michaelis-Menten kinetic theory does not, therefore, seem to be ap

12 Michaelis-Menten kinetics permit estimates of maximal survival and

13 Michaelis-Menten kinetics provides a solid framework for enzyme ki

14 Michaelis-Menten kinetics revealed a Km of 169 mum and a Vmax of 7

15 Michaelis-Menten kinetics studies revealed a classic noncompetitiv

16 Michaelis-Menten kinetics was used to treat transitions between th

17 Michaelis-Menten modeling of the single-light pulse revealed no si

18 Michaelis-Menten parameters of 4-nitrophenyl glucopyranoside hydro

19 Michaelis-Menten plots were obtained from a single reaction, yield

20 Michaelis-Menten studies indicated an allosteric mechanism of inhi

21 Michaelis-Menten transport kinetics indicates that either OCS or t

22 Michaelis-Menten, competitive inhibition, and site-directed mutage

23 species exhibit no variation and a Michaelis-Menten analysis reveals that chemistry of this reaction

24 his approach is demonstrated via a Michaelis-Menten analysis which yields a Michaelis constant, Km, o

25 Using a Michaelis-Menten approach, the oxygen binding constants for the tw

26 on(R) and glucose oxidase (GOx), a Michaelis-Menten constant (K'(m)) of 20-30 mM is obtained in the c

27 ding of the probe with TrxR with a Michaelis-Menten constant (K(m) ) of 15.89 mum.

28 protocol was shown by generating a Michaelis-Menten curve for the methylation of heterogeneous nuclea

29 ases as growth slows, exhibiting a Michaelis-Menten dependence on the abundance of the cellular trans

30 tein expression was measured and a Michaelis-Menten enzyme kinetic analysis was performed at 37 degre

31 roxy-TriBECH were best fitted to a Michaelis-Menten enzyme kinetic model.

32 -diffusion simulations including a Michaelis-Menten expression for the urease reaction with a bell-sh

33 effectively be described within a Michaelis-Menten framework.

34 A Michaelis-Menten function was fit to each cell's contrast response

35 It follows a Michaelis-Menten mechanism.

36 s more complex than expected for a Michaelis-Menten model.

37 east-squares analysis coupled to a Michaelis-Menten prognostic model was conducted to estimate rates

38 o which flux can be explained by a Michaelis-Menten relationship between enzyme, substrate, product,

39 Here we used a Michaelis-Menten substrate-based kinetics framework to explore how

40 e with time showed a good fit to a Michaelis-Menten surface cleavage model, enabling the extraction o

41 esence of their substrates, with a Michaelis-Menten-like concentration dependence.

42 etics of tethered kinases follow a Michaelis-Menten-like dependence on effective concentration.

43 Our process model combined a Michaelis-Menten-type equation of substrate availability and micro

44 Kinetic experiments delineate a Michaelis-Menten-type mechanism, with measured rate accelerations

45 s to experimental data indicated a Michaelis-Menten-type reaction having a Vmax of 1-2 microM s-1 and

46 ng curve fitting for more accurate Michaelis-Menten parameters.

47 ical rate laws, e.g., mass-action, Michaelis-Menten, Hill).

48 t maxima (Imax) of 92.55microA and Michaelis-Menten (Km) constant of 30.48microM.

49 detection limit of 0.48microM and Michaelis-Menten constant (Km) value of 44.2microM.

50 enzymatic reaction conditions, and Michaelis-Menten constants.

51 ted genetic regulatory network and Michaelis-Menten dynamics, as well as real world data sets from DR

52 gleaned from linking Arrhenius and Michaelis-Menten kinetics for both photosynthesis and soil respira

53 g nonlinear optical microscopy and Michaelis-Menten kinetics-based simulations, we isolated fatty aci

54 with respect to kinetic order and Michaelis-Menten kinetics.

55 we expanded the Dual Arrhenius and Michaelis-Menten model, to apply it consistently for all three GHG

56 metabolic control theory (MCT) and Michaelis-Menten saturation kinetics (SK).

57 ng classic enzymatic reactions and Michaelis-Menten-type kinetic analysis.

58 emonstrating both nonsaturable and Michaelis-Menten-type saturable uptake.

59 howed that V(NO) exhibits apparent Michaelis-Menten behavior for B5 and B5R.

60 .3 nA/(mM mm(2)) with the apparent Michaelis-Menten constant (K(M)(app)) derived from an L-arginine (

61 The apparent Michaelis-Menten constant (K(M)(app)) of HRP on the nano-Ni-SnO(2)

62 The apparent Michaelis-Menten constant (K(m)) and Hb adsorption in the CNT/Hb n

63 The apparent Michaelis-Menten constant (Km(app)) was 694 +/- 8 muM.

64 The apparent Michaelis-Menten constant (Km(app)) was calculated to be 1.22 mM.

65 The apparent Michaelis-Menten constant (KM(app)) was calculated to be 2.32 mM.

66 scent RNA and reduces the apparent Michaelis-Menten constant for nucleotides, suggesting that it stab

67 The apparent Michaelis-Menten constant Kapp(M) value was 21 microM.

68 The apparent Michaelis-Menten constant of Hb on the PpPDA@Fe3O4 nanocomposite w

69 the urea biosensor, with apparent Michaelis-Menten constants (KM,app), obtained from the creatinine

70 From these results, apparent Michaelis-Menten constants as well as the kinetic parameters k(1)

71 cid concentration and the apparent Michaelis-Menten kinetic parameter (Km) is estimated to be about 0

72 The apparent Michaelis-Menten kinetic parameters determined by this DGAT SPA me

73 lts based on the measured apparent Michaelis-Menten parameters Km and Vmax.

74 cyt c samples demonstrate apparent Michaelis-Menten parameters of Vm = 0.34 fmol/s and kcat/Km on the

75 ) (3.4 nmol L(-1)) and an apparent Michaelis-Menten rate constant of 3.2x10(-6)molL(-1), which is con

76 We applied Michaelis-Menten kinetics featuring regulatory factors to describe

77 By applying Michaelis-Menten kinetic analysis to C. difficile spore germinatio

78 ver) pyrophosphate exchange assay, Michaelis-Menten kinetics are observed.

79 y the enzyme activity, the assumed Michaelis-Menten mechanism can no longer be valid.

80 orm with the mechanistically-based Michaelis-Menten kinetics for enzymatic processes, which has provo

81 inolates respond similarly to both Michaelis-Menten and specific activity analyses.

82 imulations on the covalently bound Michaelis-Menten complex.

83 avage rates (V(max)) calculated by Michaelis-Menten analysis differed by more than 100-fold under mul

84 -response functions were fitted by Michaelis-Menten equations and showed significantly lower retinal

85 abolites are usually determined by Michaelis-Menten kinetic theory.

86 h substrates could be described by Michaelis-Menten kinetics.

87 ver signals were used to calculate Michaelis-Menten kinetics with a K(m) = 25 microM.

88 al rate fits can affect calculated Michaelis-Menten or EC(50)/IC(50) kinetic parameters.

89 e largely dominated by the classic Michaelis-Menten (MM) uptake functional form, whose constant param

90 recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a

91 We applied the classic Michaelis-Menten enzyme kinetics to demonstrate a novel mathematic

92 ctivity is consistent with classic Michaelis-Menten kinetics.

93 es not behave according to classic Michaelis-Menten kinetics.

94 The enzyme exhibits classical Michaelis-Menten kinetics and acts cooperatively with a Hill coeff

95 ed on a hybrid framework combining Michaelis-Menten and mass action kinetics for the mitotic interact

96 fusion equation with a competitive Michaelis-Menten equation.

97 e oxidation assuming one-component Michaelis-Menten kinetics.

98 ter described with a two-component Michaelis-Menten model, indicating a high-affinity component with

99 han 5 min, resulting in conclusive Michaelis-Menten and inhibition curves.

100 rable accuracy to the conventional Michaelis-Menten formalism.

101 complexity beyond the conventional Michaelis-Menten scheme, which unrealistically forbids product reb

102 The enzyme demonstrated Michaelis-Menten kinetics in an NADPH oxidation assay, but a hydro

103 The reaction demonstrated Michaelis-Menten kinetics with a K(m) for oleoyl-CoA of 21 microm.

104 abeled RNA/DNA duplex demonstrated Michaelis-Menten kinetics with a Km value of 9.6+/-2.8 nM.

105 exploited the abundance-dependent Michaelis-Menten kinetics of trypsin digestion to selectively dige

106 as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibi

107 monstrated to accurately determine Michaelis-Menten parameters for the cleavage reaction catalyzed by

108 riments with previously determined Michaelis-Menten constants (Kms) for the enzyme activity.

109 Using this assay, we determined Michaelis-Menten kinetic constants (K(m), k(cat), and k(cat)/K(m))

110 NDC1 displayed Michaelis-Menten kinetics and was markedly inhibited by dicumarol,

111 PduX displayed Michaelis-Menten kinetics with respect to both ATP and l-threonine

112 lar weight oligomers and displayed Michaelis-Menten kinetics.

113 c for catalytic activity, displays Michaelis-Menten kinetics, and is inhibited by S-adenosyl-homocyst

114 The two Ptr4CLs exhibited distinct Michaelis-Menten kinetic properties.

115 elocities V(max) and the effective Michaelis-Menten constants K(M) under physiologically relevant vol

116 common two-step rapid equilibrium Michaelis-Menten mechanism.

117 tions (+/-cytochrome b(5)) exhibit Michaelis-Menten kinetics.

118 ptake by transporters that exhibit Michaelis-Menten kinetics.

119 Clarithromycin transport exhibited Michaelis-Menten kinetics and was inhibited below 37 degrees C.

120 tes CCK8 and vasopressin exhibited Michaelis-Menten kinetics independent of membrane cholesterol cont

121 ugh the Km(app) (apparent (fitted) Michaelis-Menten constant) of F-actin speed with ATP titration sug

122 -chain (C14-C18) substrates follow Michaelis-Menten kinetics, whereas short and medium chains (C8-C12

123 Influx followed Michaelis-Menten kinetics for NH3 (but not NH4(+)), as a function

124 GE2/glutathione transport followed Michaelis-Menten kinetics irrespective of cholesterol.

125 talyzed nitrite reduction followed Michaelis-Menten kinetics under anaerobic conditions.

126 H(+) gradient dissipation followed Michaelis-Menten kinetics, suggesting the involvement of mediated

127 of various ceramides and followed Michaelis-Menten kinetics.

128 ion, the adduct formation followed Michaelis-Menten kinetics.

129 or could be described by a fractal Michaelis-Menten model with a catalytic efficiency nearly 17% bett

130 From Michaelis-Menten analysis, HAWS has a similar K(m) (Michaelis cons

131 4,6-TCP and 2,4,6-TBP deviate from Michaelis-Menten kinetics at high concentrations.

132 f systems matching classical (e.g. Michaelis-Menten, Hill, Adair) scenarios in the infinite-size appr

133 e a strategy to convert the graded Michaelis-Menten response typical of unregulated enzymes into a sh

134 Purified lipase had Michaelis-Menten constant (Km) and catalytic constant (kcat) of 0.

135 ive analyses using a heterogeneous Michaelis-Menten model.

136 constant based on a heterogeneous Michaelis-Menten model.

137 uitin chain assembly by hyperbolic Michaelis-Menten kinetics with respect to Ubc5B approximately ubiq

138 havior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent with a spec

139 e upon binding to CA II, including Michaelis-Menten kinetics of 4-nitrophenyl acetate esterase cleava

140 Interestingly, Michaelis-Menten kinetics suggested that V477D had a 12-fold lower

141 ation rate, production rate, Kcat, Michaelis-Menten constant, etc.) and the initial concentrations.

142 orane so that saturation kinetics (Michaelis-Menten type steady-state approximation) operate during c

143 kinetics, classic enzyme kinetics (Michaelis-Menten, Briggs-Haldane, and Botts-Morales formalisms), a

144 rates and/or by sufficiently large Michaelis-Menten constants and sufficiently low amounts of total s

145 acetate buffers resulted in larger Michaelis-Menten constants, up to 14.62 +/- 2.03 mM.

146 determined from graphics of linear Michaelis-Menten equation, and it was found that investigated reac

147 A low Michaelis-Menten constant (K(m)) of 0.12 mM, indicate that the imm

148 (392 mA cm(-2) M(-1)) and a lower Michaelis-Menten constant (0.224 mM).

149 Furthermore, we have measured Michaelis-Menten kinetics on these highly active constructs, revea

150 crofluidic technique for measuring Michaelis-Menten rate constants with only a single experiment.

151 C(50) values as low as 0.5 microM; Michaelis-Menten analysis was performed for two cases and confirme

152 tion experiments show that the net Michaelis-Menten constant (6.1+/-1.5 mM) is in between GLUT2 and G

153 been proposed to describe the non-Michaelis-Menten behavior of human glucokinase.

154 E3 rates and show that, due to non-Michaelis-Menten behavior, the maximal flux is different compared

155 l tools for enzymes displaying non-Michaelis-Menten kinetics are underdeveloped, and transient-state

156 ACD showed sigmoidal, non-Michaelis-Menten kinetics for actin (K(0.5) = 30 microM) reflectin

157 ome P450 3A4 (CYP3A4) displays non-Michaelis-Menten kinetics for many of the substrates it metabolize

158 e), we unexpectedly discovered non-Michaelis-Menten kinetics in short time-scale measurements that ar

159 We described non-Michaelis-Menten kinetics with equations containing parameters equ

160 e crucial for the emergence of non-Michaelis-Menten kinetics.

161 The nonlinear Michaelis-Menten (MM) and Hill models best described the data acro

162 The rotation rates obeyed Michaelis-Menten kinetics with a maximal rotation rate (Vmax) of 1

163 ubstrate by PTPN1 and PTPN2 obeyed Michaelis-Menten kinetics, with KM values of 770 +/- 250 and 290 +

164 K, and thermolysin) while obeying Michaelis-Menten kinetics.

165 The catalysis reaction obeys Michaelis-Menten kinetics and exhibits competitive inhibition, and

166 dependence of motor velocity obeys Michaelis-Menten kinetics with K(M,ATP) = 35 +/- 5 muM.

167 The observed Michaelis-Menten constant (Km) and catalytic constant (Kcat) of th

168 r application to the evaluation of Michaelis-Menten and EC(50)/IC(50) kinetic parameters, as well as

169 mol/cm(2)) and the small value of Michaelis-Menten constant (0.76 mM) confirmed an excellent loading

170 he low value of 0.13 x 10(-4) M of Michaelis-Menten constant (K(m)) indicate the enhanced affinity of

171 A lower value of Michaelis-Menten constant (Km), of 0.062 mM for the covalently cou

172 is enables rapid quantification of Michaelis-Menten constants (KM) for different substrates and ultim

173 Determination of Michaelis-Menten constants for the substrates with Ultra-Glo indic

174 Linear and nonlinear fits of Michaelis-Menten inhibition models were used to determine apparent

175 systems in plants with the use of Michaelis-Menten kinetic modeling.

176 in literature on the evaluation of Michaelis-Menten kinetic parameters for immobilized enzymes in mic

177 characterized in vitro in terms of Michaelis-Menten kinetics (V(MAX) and K(M)), sensitivity (linear r

178 liar Briggs-Haldane formulation of Michaelis-Menten kinetics derives from the outer (or quasi-steady-

179 Together with the disappearance of Michaelis-Menten kinetics on the expanded pi-surfaces of perylened

180 ions of the hyperbolic response of Michaelis-Menten kinetics x/(K+x), with fluctuating K or stochasti

181 the individual interactions are of Michaelis-Menten type.

182 effect of multiple active sites on Michaelis-Menten compliant rate accelerations in a porous capsule

183 metal reduction is often based on Michaelis-Menten equations.

184 A mechanism based on Michaelis-Menten kinetics with competitive inhibition is proposed

185 " kinetic rate constants, based on Michaelis-Menten kinetics, can superficially show a dependence on

186 erential equation systems based on Michaelis-Menten kinetics.

187 flux (Jint) followed first-order (Michaelis-Menten) kinetics with a calculated maximum internalizati

188 dels were considered: first-order; Michaelis-Menten; reductant; competition; and combined models.

189 temperature dependency of the PEPc Michaelis-Menten constant for its substrate HCO3 (-), and there is

190 E-stimulated ATP hydrolysis rates, Michaelis-Menten constants for disassembly, and SNAP-SNARE binding

191 ion of microscopic reaction rates, Michaelis-Menten constants, and biochemical concentrations.

192 ch as decay rates, reaction rates, Michaelis-Menten constants, and Hill coefficients.

193 olishes cooperativity and restores Michaelis-Menten kinetics, while reducing the k(cat) value of the

194 nitial rate fits and the resulting Michaelis-Menten or EC(50)/IC(50) kinetic model fits, as well as h

195 se levels and calculate reversible Michaelis-Menten (MM) kinetic parameters.

196 h exhibits prototypical reversible Michaelis-Menten kinetics.

197 were calculated using a reversible Michaelis-Menten model.

198 s drastically alter the reaction's Michaelis-Menten rate equations.

199 eta-apo-14'-carotenal) do not show Michaelis-Menten behavior under the conditions tested.

200 mmon BSEP variants p.444V/A showed Michaelis-Menten kinetics irrespective of membrane cholesterol, wh

201 Both enzymes showed Michaelis-Menten kinetics with the K(m) lower for protein than for

202 n the colorimetric assay and shows Michaelis-Menten kinetic behavior using Kraft lignin as a substrat

203 lations, on average, follow simple Michaelis-Menten curves when species are randomly deleted.

204 hesis rates are governed by simple Michaelis-Menten dependence on [ATP] and [GTP] (K(m)(ATP), 27 +/-

205 *MtCM exhibits simple Michaelis-Menten kinetics with a Km of 0.5 +/- 0.05 mM and a k(cat

206 urve than that observed for simple Michaelis-Menten kinetics.

207 tained upon applying DRA to simple Michaelis-Menten type proteomic and gene regulatory systems.

208 ork from the Hwa lab, a simplified Michaelis-Menten model suggested that the decrease in k(trl) arise

209 A two-stage, Michaelis-Menten-type kinetic model is proposed by considering the

210 In contrast, standard Michaelis-Menten fitting of the decrease in molecule numbers with

211 e poorly accounted for by standard Michaelis-Menten kinetics, but require more detailed mass action f

212 This allows us to use standard Michaelis-Menten theory to analyze the time evolution.

213 tive framework for doing so is the Michaelis-Menten (M-M) model, which is grounded on two assumptions

214 er (BV) electrode kinetics and the Michaelis-Menten (MM) formalism for enzymatic catalysis, with the

215 by a simple kinetic principle: the Michaelis-Menten (MM) model.

216 For over a century, the Michaelis-Menten (MM) rate law has been used to describe the rates

217 We discuss how parameters in the Michaelis-Menten approximation and in the underlying ODE network c

218 predominantly ionic, forces in the Michaelis-Menten complex formation.

219 actam carboxyl moiety makes in the Michaelis-Menten complex.

220 revealed by the high value of the Michaelis-Menten constant (79.3 muM).

221 alues similar to or lower than the Michaelis-Menten constant (K(m)) values of ATP.

222 The Michaelis-Menten constant (K(m)) was determined as 3.3 mM.

223 The low value of the Michaelis-Menten constant (K(m)=0.34 mM) indicates the high affini

224 The Michaelis-Menten constant (Km) and catalytic constant (kcat) value

225 tory proton currents, estimate the Michaelis-Menten constant (Km) of PR (10(3) photons per second/nm2

226 The Michaelis-Menten constant (Km) value of Hb at the modified electro

227 The Michaelis-Menten constant (Km) was found to be 1.3 nM.

228 The low value of the Michaelis-Menten constant (Km=0.47 mM) indicates the high affinity

229 Go6976 progressively increased the Michaelis-Menten constant and decreased the Hill coefficient witho

230 n(-1), P < 0.05) and increased the Michaelis-Menten constant K(M) (204 +/- 6 n(M) to 478 +/- 50 nM, P

231 The Michaelis-Menten constant, KM , for PO4 remained constant under di

232 concentrations greatly exceeds the Michaelis-Menten constant.

233 (here k(cat) and k(uncat) are the Michaelis-Menten enzymatic rate constant and observed uncatalyzed

234 ctivity measurements that obey the Michaelis-Menten equation are well established.

235 pong-pong) mechanism comprises the Michaelis-Menten equation for the reactions of NADH and APAD(+), s

236 The Michaelis-Menten equation has been widely used for over a century

237 The Michaelis-Menten equation has played a central role in our underst

238 olecular system, which follows the Michaelis-Menten equation if and only if there is no enzyme-substr

239 The Michaelis-Menten equation provides a hundred-year-old prediction b

240 We apply the Michaelis-Menten equation to describe the productive states formed

241 sing substrate mass transport, the Michaelis-Menten equation, and interfacial electron transfer kinet

242 The Michaelis-Menten kinetic constant (Km) and maximum reaction veloci

243 roducing our model in terms of the Michaelis-Menten kinetic framework, we determine that these result

244 hydrolysis is consistent with the Michaelis-Menten kinetic model.

245 talysis properties that fit in the Michaelis-Menten kinetic model.

246 of mass-transfer resistances, the Michaelis-Menten kinetic parameters are shown to be flow independe

247 or comparison, we also measure the Michaelis-Menten kinetics of ADAMTS13 cleavage of wild-type VWF in

248 lyzed by these nanorods follow the Michaelis-Menten kinetics.

249 trimolecular system reduces to the Michaelis-Menten kinetics.

250 ic system is more complex than the Michaelis-Menten kinetics.

251 progress curves conforming to the Michaelis-Menten mechanism E+Sright harpoon over left harpoonES-->

252 The Michaelis-Menten model describing the kinetics of enzymatic reacti

253 In addition, deviations from the Michaelis-Menten model in DNA competition experiments suggested an

254 ted characteristics similar to the Michaelis-Menten model of an enzymatic electrode, due to the use o

255 kinetics: the rate data obeyed the Michaelis-Menten model of enzyme kinetics, and competitive inhibit

256 over rates of the enzyme using the Michaelis-Menten model.

257 the supramolecular host obeys the Michaelis-Menten model.

258 e liver were well-described by the Michaelis-Menten model.

259 membrane-bound NDH-2 followed the Michaelis-Menten model; however, the maximum turnover was only ach

260 rated a consistent decrease in the Michaelis-Menten parameter kM with increasing soil available N, in

261 The Michaelis-Menten parameters (Km and Vmax) for the glucuronidation

262 ism could not be identified as the Michaelis-Menten parameters and maximal rate constants were not si

263 rate preference by determining the Michaelis-Menten parameters describing the activity of wtOGT and O

264 At its optimal pH of 4.0, the Michaelis-Menten parameters of K(m) and k(cat) for FlgJ from S. en

265 of the temperature response of the Michaelis-Menten parameters supports the use of substrate-based ki

266 Based on the Michaelis-Menten plots, the Km with casein as substrate was 16.8mu

267 er, its analysis has relied on the Michaelis-Menten reaction mechanism, which remains widely used des

268 of the founding hypotheses of the Michaelis-Menten reaction scheme, MM.

269 rameter kinetic model based on the Michaelis-Menten scheme with a time-dependent activity coefficient

270 ssumptions more realistic than the Michaelis-Menten scheme.

271 librium constant obtained from the Michaelis-Menten treatment (ca. 29-39) are consistent with ultra-h

272 s general equation encompasses the Michaelis-Menten, Hill, Henderson-Hasselbalch, and Scatchard equat

273 These methods are not limited to Michaelis-Menten assumptions, and our conclusions hold for enzymes

274 0-10 mM NaF, and data were fit to Michaelis-Menten curves.

275 This activity conformed to Michaelis-Menten kinetics but was unresponsive to substrates or ac

276 sterol content shifted E17betaG to Michaelis-Menten kinetics.

277 ions for fitting the H-function to Michaelis-Menten kinetics.

278 l-Trp kinetics from allosteric to Michaelis-Menten with a concurrent decrease in substrate affinity

279 talytic behavior of Th-MOF tracked Michaelis-Menten equation and the affinity of this nanozyme to the

280 ular systems follow enzymatic-type Michaelis-Menten kinetics, with competitive product inhibition.

281 pproach similar to that used under Michaelis-Menten kinetics.

282 ated that biodegradation underwent Michaelis-Menten kinetics rather than first-order kinetics.

283 c parameters were determined using Michaelis-Menten and Lineweaver-Burk plots.

284 netics of AAO were described using Michaelis-Menten equation.

285 e human proximal tubule (PT) using Michaelis-Menten kinetics and molar urinary protein measurements t

286 70 degrees C) were described using Michaelis-Menten model and first order reaction model, respectivel

287 ive enzyme kinetics analysis using Michaelis-Menten parameters is possible through interpretation of

288 When using Michaelis-Menten rate expressions to model PINs, care must be exer

289 data including enzymatic velocity, Michaelis-Menten kinetic parameters, and mechanisms of enzymatic i

290 In vitro Michaelis-Menten analyses on a series of alkylated bases show high

291 rugged Escherichia coli cells with Michaelis-Menten binding of drugs that inactivate ribosomes.

292 ima ranged from pH 5.4 to 6.4 with Michaelis-Menten constants between 0.84 +/- 0.09 and 4.6 +/- 0.7 m

293 cies reactive transport model with Michaelis-Menten kinetics was developed to explain the concentrati

294 osylase assays are consistent with Michaelis-Menten kinetics.

295 d were found to be consistent with Michaelis-Menten kinetics.

296 nd the results were evaluated with Michaelis-Menten saturation kinetics.

297 inetic mass balance equations with Michaelis-Menten type expressions for reaction rates and transport

298 reactions ranging from mass action, Michales-Menten-Henri (MMH) and Gene-Regulation (GRN) to Monod-Wy

299 reening results were validated with Michalis-Menten kinetic analyses of 21 oligopeptide aminomethyl-c

300 Michelis-Menten kinetic studies indicated a noncompetitive mechan