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 analyses demonstrated reduced contrast gain of th

6 Michaelis-Menten analysis of kinase inhibition by a selected scFv

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

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

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

10 Michaelis-Menten kinetic constants for the reaction occurring in s

11 Michaelis-Menten kinetic parameters from amino acid activation ass

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

13 Michaelis-Menten kinetics emerge with reduction catalyzed by force

14 Michaelis-Menten kinetics permit estimates of maximal survival and

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

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

17 Michaelis-Menten kinetics studies revealed a classic noncompetitiv

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 Zn2+ or Cd2+ by a hyperbola with a Michaelis-Menten constant (K(m)) of 104.9 +/- 5.4 microm and 90.1

28 ime dependent and saturable with a Michaelis-Menten constant (Km) of 27+/-3 microM.

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

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

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

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

33 response functions were fit with a Michaelis-Menten equation to derive R(max), the maximum response a

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

35 effectively be described within a Michaelis-Menten framework.

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

37 (1,2-dihexanoyl-sn-glycerol), in a Michaelis-Menten manner.

38 It follows a Michaelis-Menten mechanism.

39 the OPPP, ToTal1 does not follow a Michaelis-Menten mode of catalysis which has implications for its

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

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

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

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

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

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

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

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

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

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

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

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

52 enzymatic reaction conditions, and Michaelis-Menten constants.

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

54 yzed using rat control plasma, and Michaelis-Menten enzyme kinetic analysis was performed at 37 degre

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

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

57 ohexanol (vesamicol) with ACh, and Michaelis-Menten parameters were determined for [(3)H]ACh transpor

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

59 s for transcription regulation and Michaelis-Menten type or delay terms for posttranslation regulatio

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

61 .3 nA/(mM mm(2)) with the apparent Michaelis-Menten constant (K(M)(app)) derived from an L-arginine (

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

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

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

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

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

67 ated and found to have an apparent Michaelis-Menten constant (KM) of 1.2 mM for the indolyl galactopy

68 inward transport with the apparent Michaelis-Menten constant and a maximum transport rate of 51 micro

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

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

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

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

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

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

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

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

77 ) (3.4 nmol L(-1)) and an apparent Michaelis-Menten rate constant of 3.2x10(-6)molL(-1), which is con

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

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

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

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

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

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 sured on APM gels and evaluated by Michaelis-Menten kinetics.

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

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 es not behave according to classic Michaelis-Menten kinetics.

93 ctivity is consistent with classic Michaelis-Menten kinetics.

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

95 I by Galpha(s) displayed classical Michaelis-Menten kinetics, whereas AC V activation by Galpha(s) wa

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

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

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

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

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

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

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

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

108 ver a broad pH range and displayed Michaelis-Menten kinetics with a K(m) of 86 microm.

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

110 DGKA displayed Michaelis-Menten kinetics with respect to bulk substrate concentra

111 lar weight oligomers and displayed Michaelis-Menten kinetics.

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

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

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

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

116 ptake by transporters that exhibit Michaelis-Menten kinetics.

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

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

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

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

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

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

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

124 the rate of NO production followed Michaelis-Menten kinetics, and oxygen functioned as a competitive

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

126 ate of nitrite production followed Michaelis-Menten kinetics, while NO generation rates increased lin

127 of various ceramides and followed Michaelis-Menten kinetics.

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

129 ncision of alpha-C-Fapy.dA follows Michaelis-Menten kinetics (K(m) = 144.0 +/- 7.5 nM, k(cat) = 0.58

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

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 However, Michaelis-Menten constant was significantly increased at 30 degree

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 cs are consistent with independent Michaelis-Menten catalysis in each subunit of the Hsp90 dimer.

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

142 balance analysis, or fully kinetic Michaelis-Menten representations, metabolic control analysis, or b

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

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

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

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

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

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

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

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

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

157 indicated that CYP3A4 exhibits non-Michaelis-Menten kinetics for numerous substrates.

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

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

162 arying amounts of isoforms obeying Michaelis-Menten kinetics but with different values of Km and kcat

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

164 brucei flavoprotein (TbALO) obeys Michaelis-Menten kinetics and can utilize both L-galactono-gamma-l

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

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

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

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

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

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

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

175 , the well-established concepts of Michaelis-Menten kinetics and Langmuir binding isotherms are combi

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

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

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

179 the individual interactions are of Michaelis-Menten type.

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

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

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

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

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

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

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

187 anched or rapid-equilibrium random Michaelis-Menten systems containing multiple isotopically sensitiv

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

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

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

191 er, the constraints do not require Michaelis-Menten constants for most enzymes, and they only require

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

193 peroxide concentration, revealing Michaelis-Menten kinetics and K(m) = 55 microm.

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

195 were calculated using a reversible Michaelis-Menten model.

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

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

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

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

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

201 a generation assays showed similar Michaelis-Menten constant (K(m), apparent) values for thrombin-cat

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

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

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

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

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

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

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

209 result obtained from the standard Michaelis-Menten treatment.

210 t has been limited to steady-state Michaelis-Menten approaches or to compartmental models, neither of

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

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

213 d than situations described by the Michaelis-Menten and Langmuir equations.

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

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

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

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

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

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

220 of 3beta-HSD1 (Q105M1) shifts the Michaelis-Menten constant (Km) for 3beta-HSD substrate and inhibit

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

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

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

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

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

226 ed that C-1-P had no effect on the Michaelis-Menten constant, K(m)(B), but decreased the dissociation

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

228 concentrations greatly exceeds the Michaelis-Menten constant.

229 constants are similar, as are the Michaelis-Menten constants for substrate hydrolysis.

230 The Michaelis-Menten constants Vmax, KM, and kcat of Atm1-C were measu

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

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

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

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

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

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

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

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

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

240 Using the Michaelis-Menten equation, the rate of the reaction can be correla

241 on [ATP] was well described by the Michaelis-Menten equation.

242 We describe limitations in the Michaelis-Menten kinetic analysis of Dnmt1 and suggest alternative

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

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

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

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

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

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

249 trimolecular system reduces to the Michaelis-Menten kinetics.

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

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

252 The Michaelis-Menten mass action reaction is used to model P-gp transp

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

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

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

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

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

258 e at interstitial pH = 7.4 fit the Michaelis-Menten model with k cat/Km = 74.9 +/- 10.9 M(-1) s(-1).

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

260 the supramolecular host obeys the Michaelis-Menten model.

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

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

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

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

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

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

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

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

269 s using the integrated form of the Michaelis-Menten rate equation.

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

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

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

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

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

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

276 0-10 mM NaF, and data were fit to Michaelis-Menten curves.

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

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

279 sterol content shifted E17betaG to Michaelis-Menten kinetics.

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

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

282 the reaction which follows typical Michaelis-Menten kinetics (K(m) of 0.6 microM, and a V(max) of 30

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

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

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

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