ライフサイエンスコーパス: Vmax

1 Vmax >/=5 m/s at the time of AS diagnosis identifies pat

2 Vmax for [59Fe]-enterobactin (0.15 pMol per 10(9) cells

3 Vmax is elevated, with no change in Km.

4 Vmax values for all variants were similar to the WT valu

5 ith severe AS (aortic valve area </=1 cm(2), Vmax >/=4 m/s) and preserved left ventricular ejection f

6 lues for kinetic constants Km(app) (6.60mM), Vmax (17.69mumol/min mg protein) and kcat(app) (1987.64s

7 ure of 41 degrees C, a Km of 5 microM, and a Vmax of 11,111 micromol of As(V) reduced min(-1) mg of p

8 nten kinetics revealed a Km of 169 mum and a Vmax of 7550 nmol/mg/min for the substrate AMP.

9 e peptide substrate (Km = 12.4 microM) and a Vmax value (10.3 pmol/min) that was only 3-fold lower th

10 m as a preferred substrate, XynC exhibited a Vmax of 59.9 units/mg XynC, a Km of 1.63 mg MeGAXn/ml, a

11 ed a Michaelis-Menten-type reaction having a Vmax of 1-2 microM s-1 and a Km of around 10 nM.

12 e oxidative cleavage of beta-carotene with a Vmax = 197.2 nmol retinal/mg BCO1 x h, Km = 17.2 muM and

13 the Km for L-arginine is 3.14 microM with a Vmax of 0.14 micromol mg-1 min-1, whereas Ki values of 0

14 abeled substrate was 38 +/- 18 microM with a Vmax of 0.4 +/- 0.2 microM/min and a kcat of 3900 s-1.

15 exhibited significant ATPase activity with a Vmax of 82 +/- 32 nmol min-1 mg-1.

16 MR imaging accuracy, or A, calculated as A = Vmax/Vh, were evaluated using generalized linear mixed m

17 The actin-activated ATPase activities (Vmax) of asymmetric HMMs were only 21.8 and 8.4% of the

18 low actin-activated Mg(2+)-ATPase activity (Vmax = 4 s(-1)), although their affinities for actin wer

19 arent Km of 0.4 mM, and a specific activity (Vmax) of 20.0 mumol min(-1) mg(-1) corresponding to a kc

20 of diverse aromatic and aliphatic aldehydes: Vmax values varied <5-fold, but Km values ranged from 3.

21 le-blind approach, Qaw along with FEV(1) and Vmax(50) were determined before and after a 2-week treat

22 FEV(1) and Vmax(50) were not changed by any of the treatments.

23 Km(Cbl) = 4.1 microm, kcat = 0.06 s(-1), and Vmax = 105 nm min(-1).

24 Km(ATP) = 10 microm, kcat = 0.03 s(-1), and Vmax = 54.5 nm min(-1).

25 Blueberry PPO showed a Km of 15mM and Vmax of 2.57 DeltaA420nm/minx10(-1), determined with cat

26 for the D778G mutant, whereas ttp, t0.5 and Vmax were unchanged for the G741R mutant.

27 Km with casein as substrate was 16.8muM and Vmax was 82.6muM/min.

28 mode) with the Deltatrac MBM-100 (Datex) and Vmax Encore 29n (SensorMedix) was performed in postabsor

29 p and t0.5 were significantly decreased, and Vmax was increased for the D778G mutant, whereas ttp, t0

30 a mixed type inhibition as km increased and Vmax decreased.

31 nd xanthine oxidase reveals similar Kcat and Vmax values but more sustained NO formation from mARC, p

32 The apparent Km and Vmax for lyso-PE 18:1 were 116 microM and 875 micromol m

33 Using the assay, the KM and Vmax of recombinant CSE enzyme were determined to be 11.

34 The apparent Km and Vmax of the amylase were 2.7 mg/ml and 34.30 u/min/mg of

35 of enzyme kinetics revealed that the Km and Vmax of the purified recombinant MzASMT9 protein for mel

36 lyses were conducted to determine the Km and Vmax parameters of these two hydrolysates using the Line

37 s active as a hexamer with values for Km and Vmax that agree well with those reported for a bovine ho

38 onessential activators effecting both KM and Vmax values (Vmax =maximum rate of reaction).

39 ificant differences were observed for Km and Vmax values for 4-methyl-7-hydroxycoumarin and 4-nitroph

40 n either HEK293 or HeLa cells had low Km and Vmax values for As(GS)3, similar to HeLa wild-type (WT)

41 r ATP hydrolysis, yet relatively high Km and Vmax values for ATP hydrolysis, and ATPase activity is o

42 The Km and Vmax values for purified Xyl2 were 9.6mg/mL and 28.57mum

43 g mimosine degradation, with apparent Km and Vmax values of 1.16x10(-4) m and 5.05x10(-5) mol s(-1) m

44 The reaction exhibited Km and Vmax values of 24 microM and 0.14 nmol x min(-1) x cm(-2

45 cine and L-phenylalanine and provided Km and Vmax values of approximately 16 microM and 350-480 pmol/

46 The Km and Vmax values of CRCK1 for ATP are 1 microm and 33.6 pmol/

47 The Km and Vmax values of immobilized invertase were found to be 39

48 M and 23mM/min, respectively, whereas Km and Vmax values of immobilized trypsin were 7.88mM and 18.3m

49 The Km and Vmax values on beechwood xylan were determined to be 19.

50 The Km and Vmax values toward sphingosine were 23.75 microM and 208

51 thermore, year-to-year variability in Km and Vmax values was significant.

52 Apparent Km and Vmax values were 17 microM and 7.2 nmol x min(-1) x cm(-

53 Km and Vmax values were 79.37mg/ml and 5.13U/ml, respectively a

54 For guaiacol, the Km and Vmax values were calculated as 24.88mM and 3.23EU/mL, re

55 For H2O2, the Km and Vmax values were calculated as 3.247mM and 0.799EU/mL, r

56 strated significant decreases of both Km and Vmax values, suggesting a mechanism of uncompetitive inh

57 in (MBP) as substrates, with matching Km and Vmax values.

58 no effect on basal kinase activity or Km and Vmax values; however, PKGIalpha containing the C43S muta

59 The Michaelis-Menten parameters (Km and Vmax) for the glucuronidation of 4-methyl-7-hydroxy coum

60 stimulates degradation via changes in Km and Vmax, and that major alterations in the length of the 48

61 Cys showed significant differences in Km and Vmax.

62 apparent Michaelis-Menten parameters Km and Vmax.

63 Km for the substrate is 2.4 x 10(-4) m, and Vmax is 4.7 x 10(-5) m/s.

64 mbryonic kidney 293 (HEK) (Km 3.8 microM and Vmax 307 pmol/mg per minute) and HeLa (Km 0.32 microM an

65 /mg per minute) and HeLa (Km 0.32 microM and Vmax 42 pmol/mg per minute) cells.

66 revealed the Km value of 27+/-1.5 microM and Vmax value of 157+/-14 pmol/mg/min.

67 trated Km values of 68.7 and 53.6 microM and Vmax values of 356 and 154 nmols/mg/min for ADMA and L-N

68 wild-type transport, with Km=1.2 microM and Vmax=0.5 pmol/10(7)cells/min.

69 we established an apparent Km=0.9 microM and Vmax=1.8 pmol/10(7)cells/min for FbpABC-mediated transpo

70 hosphatase activity (Km 27.38 +/- 3.1 mM and Vmax 0.077 +/- 0.005 mumol min(-)(1) mg protein(-)(1)) a

71 g arsenate reductase (Km 16.0 +/- 1.2 mM and Vmax 5.6 +/- 0.31 mumol min(-)(1) mg protein(-)(1)) and

72 HA reductase activity at a Km of 0.15 mM and Vmax of 35 nmol/min.

73 theinase are KM,C/alpha = 4.4 +/- 1.1 mM and Vmax,C = 29 +/- 3 nM/s, where alpha is the percentage yi

74 st suitable substrate (Km=0.56+/-0.07 mM and Vmax=53.15+/-2.03 UPPO mL(-1) min(-1)).

75 -dGMP with a Km of approximately 9.5 muM and Vmax of approximately 0.04 pmol/min per ng of protein.

76 o-dGDP with a Km of approximately 50 muM and Vmax of approximately 0.9 pmol/min per ng of protein, an

77 risk was similar for Vmax 5 to 5.49 m/s and Vmax >/=5.5 m/s (P=0.93).

78 Both Vmax 5 to 5.49 m/s and Vmax >/=5.5 m/s exhibited significant excess mortality c

79 use mortality between Vmax 4 to 4.49 m/s and Vmax 4.5 to 4.99 m/s (P=0.64).

80 The specific activities, Km values, and Vmax values of adenine phosphoribosyltransferase and of

81 the theoretical isotope effects on Vmax and Vmax/Km that are predicted from the free energy profile

82 ured the kinetic isotope effects on Vmax and Vmax/Km when deuterated toluene is the substrate.

83 are 1.7 +/- 0.2 and 2.9 +/- 0.1 on Vmax and Vmax/Km, respectively; at 4 degrees C they increase slig

84 Apparent Vmax values of 6.6 +/- 0.9 to 10.7 +/- 0.1 nmol/min/ mg

85 abundant in yeast, also had a high apparent Vmax.

86 -CoA and oleoyl-CoA showed a higher apparent Vmax.

87 inhibitors are those with very low apparent Vmax and very low Km values.

88 ssays showed that MDPD enhanced the apparent Vmax of AtFAAH but did not alter the affinity of AtFAAH

89 Both compounds increased the apparent Vmax of recombinant FAAH proteins from both plant (Arabi

90 on of cis-DCE to chloride ions, the apparent Vmax/Km for the Escherichia coli strain expressing recom

91 increase in cone a- and b-wave amplitude at Vmax and in rod b-wave amplitude at Vmax was observed in

92 t Vmax, whereas enhanced b-wave amplitude at Vmax was found in GSK3beta(+/-) mice.

93 itude at Vmax and in rod b-wave amplitude at Vmax was observed in GSK3alpha-KO mice.

94 ance, decreased rod ERG (b-wave amplitude at Vmax) is a biological endophenotype in young offspring a

95 served a decrease in rod b-wave amplitude at Vmax, whereas enhanced b-wave amplitude at Vmax was foun

96 ing substrate concentrations after attaining Vmax for certain chemicals.

97 no difference in all-cause mortality between Vmax 4 to 4.49 m/s and Vmax 4.5 to 4.99 m/s (P=0.64).

98 we aimed to assess the relationship between Vmax and mortality and determine the best threshold to d

99 demonstrate the strong relationship between Vmax and mortality in patients with severe AS and preser

100 Both Vmax 5 to 5.49 m/s and Vmax >/=5.5 m/s exhibited signifi

101 Both Vmax and kcat/KM for DMQ hydroxylation increase when DMQ

102 low as 0.015 mM and better loading capacity (Vmax=6.7x10(-6) M s(-1)).

103 atory flows at functional residual capacity (Vmax(FRC)) in 169 of these infants by the chest compress

104 the synaptosomal glutamate uptake capacity (Vmax) was reduced significantly (40%).

105 [59Fe]-apoferrichrome similarly to E. coli (Vmax=24 pMol per 10(9) cells per minute).

106 2+)/CaM-independent activity with comparable Vmax and Km values for different RLCs.

107 dly oxidize H2 at a range of concentrations [Vmax(app) = 12 nmolgdw(-1)min(-1); Km(app) = 180 nM; thr

108 The Michaelis-Menten constants Vmax, KM, and kcat of Atm1-C were measured as 1.822 micr

109 In contrast, Vmax for [(3)H]serotonin uptake and cellular localizatio

110 For [59Fe]-corynebactin, Vmax was also low (1.2 pMol per 10(9) cells per minute),

111 In contrast, mANP decreased Vmax, AP duration, and ICa,L, and these effects were com

112 f these residues to alanine, which decreases Vmax(app) and has profound effects on the Km(app) for gl

113 IXa N178A and R165A demonstrated a defective Vmax(app) for factor X activation.

114 vely), although they have slightly different Vmax values (2.55 and 0.96 micromol/min/mg, respectively

115 K48M and R73M mutants exhibit diminished Vmax values in both reaction directions (>1000-fold) wit

116 50), but strongly affected maximum efficacy (Vmax), with constrained bithiazoles 9e and 10c increasin

117 substrates, we assessed transport efficacy (Vmax) for Oat6 and Oat1.

118 f deoxy-NTPs and decreased the efficiencies (Vmax/Km) of DPs.

119 m(B) = 4.2 mol %), and catalytic efficiency (Vmax = 557 mumol/min/mg).

120 rease in carboxylation catalytic efficiency (Vmax/Km).

121 displayed significant enzymatic efficiency (Vmax/Km) with different substrates.

122 Respective estimated Vmax values (maximum metabolic rate) for these metabolit

123 Overall, the estimated Vmax and KM values were situated in the same order of ma

124 t and interpretation to obtain, for example, Vmax and Km for an enzymatic reaction in the extracellul

125 tile, and 75th percentile, respectively, for Vmax accuracy were 0.92, 0.54, and 1.85 for reader 1 and

126 Mortality risk was similar for Vmax 5 to 5.49 m/s and Vmax >/=5.5 m/s (P=0.93).

127 Values for Vmax are 220 +/- 10 and 1,500 +/- 90 nmol/min/mg in the

128 GLUT2 and GLUT8, respectively) and fructose (Vmax of 406 and 116 pmol/min/oocyte for GLUT2 and GLUT8,

129 er than maximal rates for 2-deoxy-d-glucose (Vmax of 224 and 32 pmol/min/oocyte for GLUT2 and GLUT8,

130 rved left ventricular ejection fraction have Vmax in this range, we aimed to assess the relationship

131 i) cells with a high rate of transport (high Vmax), (ii) cells with high-affinity transporters (low K

132 ex showed that this isoform conferred higher Vmax and Km values as well as higher acidic pH-dependent

133 lpha4.PP2A heterodimer had a 100-fold higher Vmax than alpha4.PP6, and neither heterodimer was active

134 ctivated ATPase rates were increased (higher Vmax) by both exon exchanges.

135 IDH mutant exhibits a 2000-fold decrease in Vmax, with increases of 15-fold in the Kms for Mn(II) an

136 e catalytic dwell and associated decrease in Vmax, with magnitudes consistent with the level of disru

137 pp)FIXa and approximately 4-fold decrease in Vmax.

138 p)FIXa and approximately 10-fold decrease in Vmax; and V107A had an increase of approximately 3-fold

139 A large (100-fold) difference in Vmax accounts for nucleotide specificity (ATP vs CTP), d

140 a and a decrease of approximately 20-fold in Vmax; I90A had an increase of approximately 5-fold in Kd

141 Both an increase in Vmax and a decrease in KM caused this increase in rate.

142 d by a decrease in the Km and an increase in Vmax for both Ado and methyl-Ado.

143 large decrease in Km and a small increase in Vmax toward an ABL consensus substrate peptide.

144 The increase in Vmax was not accounted for by increases in transporter e

145 426C and K899C), resulting in an increase in Vmax with only minimal changes to Km.

146 tion is due to a GCAP2-dependent increase in Vmax without an alteration of retGC affinity for GCAP2 (

147 ulin, and was associated with an increase in Vmax without changes in Km for ATP-Mg2+.

148 ulation of GTPCH activity: a 20% increase in Vmax, 50% decrease in KmGTP, and increase in Hill coeffi

149 R141M exhibits little perturbation in Vmax [14-fold (forward) and 10-fold (reverse)] but has i

150 ide showed an approximately 50% reduction in Vmax but no change in apparent Ks.

151 and DD-CoA turnover but with a reduction in Vmax for DD-CoA, impairing overall activity.

152 [50-fold (forward) and 85-fold (reverse)] in Vmax.

153 Activation increased Vmax of the enzyme without affecting the Km and decrease

154 The altered protein has an increased Vmax over that of Grx3, nearly the same Vmax as Grx1 whi

155 l, whereby cholesterol leads to an increased Vmax while Km remains unchanged.

156 [(3)H]dopamine uptake in mPFC, but increased Vmax for [(3)H]dopamine uptake in OFC.

157 utation decreased the EC50 5-fold, increased Vmax 2.6-fold, and decreased the Km 13-fold, whereas the

158 ate substitutions had no effect or increased Vmax Ala but not Glu substitution for Ser-497 increased

159 onstrained bithiazoles 9e and 10c increasing Vmax by 1.5-fold compared to benchmark bithiazole corr4a

160 ATPase and alters its kinetics by increasing Vmax However, unlike other family members FXYD5 appears

161 onse to P stress by significantly increasing Vmax and alphaP for both inorganic and organic P (PO4 an

162 Participants who had infant Vmax(FRC) in the lowest quartile also had lower values f

163 and Vh (P < .0001) significantly influenced Vmax accuracy (both readers).

164 ociated with a marked decrease in the influx Vmax and collapse of the transmembrane proton gradient a

165 pentakisphosphate (PP-InsP5) to (PP)2-InsP4 (Vmax = 8.3 nmol/mg of protein/min; Km = 0.34 microM).

166 respectively and the kinetic parameters (Km, Vmax and kcat) were determined to be 0.33 (mgml(-1)), 0.

167 We report the KM, Vmax, and Ea values for GTP hydrolysis and the Kd value

168 y and affinity similar to those in BTCs (low Vmax and high KM).

169 on the cell surface but caused extremely low Vmax and Km values for DA uptake, converted the inhibito

170 horter action potential duration and a lower Vmax in subepicardium compared with subendocardium cardi

171 active site are consistent with the lowered Vmax.

172 g rats correlated positively and left medial Vmax values correlated negatively with the animals' perf

173 he maximum velocity of phenytoin metabolism (Vmax) 4.6-fold (11.6-2.53 mg/hr) and reduced the overall

174 of external concentration (Km = 152 microm, Vmax = 205 micromol g(-1) h(-1)).

175 ase appears to be starch with Km 1.56 mg/mL, Vmax 1666.67 U/mg and kcat 485 s(-1) and hence is suitab

176 faster than the 2-6, and a KM of 2 +/- 1 mM (Vmax, 400 +/- 100 muM/min) was obtained for the 6'-sialy

177 linkages generated a KM value of 3 +/- 2 mM (Vmax, 900 +/- 300 muM/min) for 3'-sialyllactose.

178 A KM value of 3.3 +/- 0.8 mM (Vmax, 2100 +/- 200 muM/min) was obtained for 3'-sialylla

179 , has a high affinity for TMAO (Km = 3.3 mM; Vmax = 21.7 nmol min(-1) mg(-1) ) and only catalyses dem

180 actor IXa (Kd(app)FIXa approximately 1.1 nm, Vmax approximately 12 nm min(-1)), N89A displayed an inc

181 The pH dependence of Vmax for Arg83 and Asn328 mutants is similar to that of

182 The pH dependence of Vmax for wild-type DmTrxR has pKa values of 6.4 and 9.3

183 e previously attributed the pH dependence of Vmax to the deprotonation of the metal-bound hydroxyl of

184 8), and vasopressin displayed an increase of Vmax and a variable decrease of Km.

185 from network topology and only knowledge of Vmax values is needed to reach these conclusions.

186 With a knowledge of Vmax, the method was applied to a mixture of 2-3 and 2-6

187 turating substrate concentrations, a plot of Vmax versus free Co2+ shows sigmoidal metal activation o

188 d forms of IGF1R confirmed that the value of Vmax for Y1135F was elevated relative to wild-type IGF1R

189 e effects are 1.7 +/- 0.2 and 2.9 +/- 0.1 on Vmax and Vmax/Km, respectively; at 4 degrees C they incr

190 Comparison of the sulfur elemental effect on Vmax for ATP and CTP suggests that the chemical step is

191 in apparent Km with no significant effect on Vmax.

192 alculate a primary kinetic isotope effect on Vmax/KM of 2.0 +/- 0.2, indicating that C-H bond cleavag

193 Comparison of the sulfur elemental effect on Vmax/Km revealed differences in the mechanism by which e

194 ults with the theoretical isotope effects on Vmax and Vmax/Km that are predicted from the free energy

195 have measured the kinetic isotope effects on Vmax and Vmax/Km when deuterated toluene is the substrat

196 lf-maximum effective concentration (EC50) or Vmax contribute to AHR in asthma, but, because of high v

197 molecules-analogous to how an enzyme's Km or Vmax are medicinally targeted-holds promise as a strateg

198 ndex, or sex and sensitivity, reactivity, or Vmax.

199 ld (11.6-2.53 mg/hr) and reduced the overall Vmax by ~50%.

200 tical to the steady-state ATPase parameters (Vmax and K(ATPase)).

201 We used two classical Michaelis parameters, Vmax and KM, to kinetically characterize the rate of tra

202 ating whether the observed variation in PMCA Vmax is related to cell age.

203 Furthermore, right medial prefrontal Vmax values of CVT-performing rats correlated positively

204 o approximately 95-fold, affecting primarily Vmax The extent of activation and binding affinity corre

205 es a slower-acting, higher-affinity process [Vmax(app) = 2.5 nmolgdw(-1)min(-1); Km(app) = 50 nM; thr

206 by adjusting the maximum carboxylation rate (Vmax ) specified for tropical forests in CLM4.

207 portantly, ADAR1 increases the maximum rate (Vmax) of pre-microRNA (miRNA) cleavage by Dicer and faci

208 enten kinetics with a maximal rotation rate (Vmax) of 107 revolutions/s and a Michaelis constant (Km)

209 0.33+/-0.06mM and the maximum apparent rate, Vmax(app) as 98+/-5pMs(-1).

210 easurements of maximal Ca2+ extrusion rates (Vmax) reported only mean values in the RBC population.

211 .33 and 3.23 mm and maximal transport rates (Vmax) of 25.9 and 10.1 pmol/min/oocyte, respectively.

212 T7(F79S) shows improved xylose uptake rates (Vmax = 186.4 +/- 20.1 nmol*min(-1)*mg(-1)) that allows t

213 en paid to the inadequacy of using the ratio Vmax/KM as a measure of enzyme performance, particularly

214 A single amphetamine infusion reduced Vmax and membrane DAT levels in cocaine-naive animals, b

215 hese five variants also had the most reduced Vmax values for DOPA synthesis.

216 ared with control alpha1beta1, FXYD1 reduces Vmax and turnover rate and raises K0.5Na.

217 This modification reduces Vmax without substantially affecting substrate binding (

218 inetics of potential nitric oxide reduction (Vmax and Ks), as measured by monitoring the depletion of

219 y the maximum carboxylation rate of Rubisco (Vmax), the maximum electron transport rate (Jmax) and th

220 ased Vmax over that of Grx3, nearly the same Vmax as Grx1 while the Km remains high.

221 Ser-473 to make GC-A-8E resulted in the same Vmax, Km, and EC50 as the phosphorylated WT enzyme.

222 roton-coupled transporter and was saturable (Vmax=715+/-29 pmol/mg/min, Km=606+/-14 microM).

223 om any of the individual MR pulse sequences (Vmax) were compared with Vh (Bland-Altman analysis).

224 (t0.5), the maximum velocity of shortening (Vmax) at 1 Hz stimulation, and the tetanic fusion freque

225 Measured enzyme kinetics provided similar Vmax (0.079 mM/min) and Km (0.36 mM) values as those fou

226 o a longer lived detached state and a slowed Vmax of the ATPase (2-35-fold), indicating a slower cycl

227 indicate that MED4 has a small cell-specific Vmax but a high specific affinity (alphaP ) for P, makin

228 The Vmax of immobilized enzyme was about 2.92+/-.02mg/ml/min

229 The Vmax values for proton transport were also similar among

230 antly from PLB: 1) SLN primarily affects the Vmax of SERCA-mediated Ca(2+) uptake but not the pump af

231 nt enzyme for substrate without altering the Vmax.

232 d at pH 7.6, the Sp-CK Km is 0.25 mm and the Vmax 5.25.

233 stion decreased the Bmax for binding and the Vmax for uptake in amounts that were proportional to the

234 pH 7.6, the Km for Sp-AK is 0.32 mm and the Vmax is 2.80 microM ATP formed/min/mg of protein.

235 produced an increase in the affinity and the Vmax of K(+) transport.

236 T1 protein in subcellular fractions, and the Vmax of striatal vesicular GLU uptake.

237 their intracellular concentrations, and the Vmax values obtained with the two reductants were simila

238 at the other end of the molecule brought the Vmax of the h4xb PMCA to near that of the calmodulin-act

239 re, exhibit a similar Km toward G6P, but the Vmax of G6Pase-alpha is approximately 6-fold greater tha

240 In contrast, the Vmax value of cMLCK is orders of magnitude lower than th

241 In contrast, the Vmax values of the beta-D192N and gamma-D190N IDHs are o

242 However, these mutations decreased the Vmax of uptake to approximately 30% of wild-type.

243 different degrees, depending on the FA, the Vmax of its Ecat partner.

244 V mutations caused a greater decrease in the Vmax using the wt RNA template compared with the G1896A-

245 uptake, but also significantly increase the Vmax of hDAT for dopamine uptake.

246 ion decreased the EC50 5-fold, increased the Vmax 2.1-fold, and decreased the Km 4.7-fold.

247 The reductase increased the Vmax but not the apparent Km values of PKC betaII for my

248 with constitutively active MEK increased the Vmax of DA transport without altering Km.

249 TcuB greatly increased the Vmax of the TcuA reaction from 69 +/- 2 to 8200 +/- 470

250 inase activity of CRCK1, which increases the Vmax of CRCK1 approximately 9-fold.

251 bation of hepatocytes with 991 increases the Vmax of cyclic nucleotide phosphodiesterase 4B (PDE4B) w

252 l hDAT mutant capable of both increasing the Vmax of hDAT for dopamine uptake and disrupting the hDAT

253 utoinhibition by specifically increasing the Vmax.

254 t depleting cellular cholesterol reduced the Vmax but not the Km of the LAT1 mediated uptake of a mod

255 tification of six molecules that reduced the Vmax of substrate hydrolysis without influencing the KM.

256 for these factors 30-80-fold and reduced the Vmax values.

257 rations in the KM values for substrates, the Vmax value for dihydroxyphenylalanine (DOPA) synthesis,

258 reticulum Ca2+ uptake assays showed that the Vmax was decreased by approximately 30% although the app

259 21P/S121P PGHS-2) that has 1.7-1.8 times the Vmax of native PGHS-2 and is relatively insensitive to a

260 ation was divided into 4 groups according to Vmax (4-4.49, 4.5-4.99, 5-5.49, and >/=5.5 m/s).

261 e purified and characterized with respect to Vmax, Michaelis constants, light and dark decays, quantu

262 e two parameters may serve a similar role to Vmax, KM, and kcat in classical kinetics.

263 h that of SERT had no effect on DA transport Vmax but significantly decreased DAT substrate affinitie

264 on or high palmitoylation increase transport Vmax and suppress PKC-stimulated down-regulation.

265 ation or low palmitoylation reduce transport Vmax and enhance PKC-stimulated down-regulation, whereas

266 n increase in velocity of cystine transport (Vmax), in the absence of a change in affinity (Km).

267 d PHT2) and also showed saturable transport (Vmax=447+/-23 pmol/mg/min, Km=43+/-5.5 microM).

268 lysine 339 to alanine yielded the wild-type Vmax, but a 165-fold decrease in affinity for UDP-glucos

269 uptake revealed a decreased Km but unchanged Vmax in knock-outs.

270 Under Vmax conditions, the average time of tauclosed was simil

271 ut TH protein and TH activity (assayed under Vmax conditions) are not increased.

272 D79E DAT mutation decreased dopamine uptake Vmax by 7-fold and decreased dopamine turnover by 4-fold

273 ne (NECA) induces an increase in 5-HT uptake Vmax in rat basophilic leukemia 2H3 cells that is enhanc

274 n, dopamine release, maximal rate of uptake (Vmax), and membrane-associated dopamine transporter (DAT

275 b) decreased growth and altered iron uptake: Vmax of [59Fe]-corynebactin transport tripled in this st

276 Vh can be estimated by using Vmax in aggressive tumors or in tumors with high Likert

277 ctivators effecting both KM and Vmax values (Vmax =maximum rate of reaction).

278 ly from a reduced maximum transport velocity Vmax without affecting the binding affinity (1/Km) of th

279 severe AS based on peak aortic jet velocity (Vmax) remains unclear with a 5-m/s cutoff in US guidelin

280 and has a 2.5-fold higher Maximal Velocity (Vmax ), and five-fold lower Michaelis Constant (Km ) tha

281 tion (41%) in the apparent maximal velocity (Vmax) of CaMKII and a significant increase (22%) in appa

282 l/L 5-HT via inhibition of maximal velocity (Vmax) without any changes in apparent affinity (Km) for

283 r-506, and Ser-510 reduced maximal velocity (Vmax), whereas glutamate substitutions had no effect or

284 e the glucose affinity and maximum velocity (Vmax) of GK.

285 constant (Km) and maximum reaction velocity (Vmax) for free trypsin were 5.1mM and 23mM/min, respecti

286 ine and unloaded tissue shortening velocity (Vmax) compared with control subjects.

287 otein phenotype, slower shortening velocity (Vmax), and longer contraction and relaxation times in ad

288 chment decreased maximal transport velocity (Vmax) for [(3)H]dopamine uptake in mPFC, but increased V

289 s indicated by maximum transporter velocity (Vmax)] and an increased density of CHTs situated in syna

290 ANP increased AP upstroke velocity (Vmax), AP duration, and ICa,L similarly in wild-type and

291 ction in overall activity (maximal velocity, Vmax), particularly skewing the balanced hydrolysis of i

292 In the presence of factor VIIIa, Vmax(app) varied in proportion to the predicted factor I

293 with novel omnipolar peak-to-peak voltages (Vmax) in sinus rhythm (SR) and AF.

294 benzoyl-dl-arginyl-rho-nitroanilide, whereas Vmax was 0.056+/-0.001nmolmin(-1).

295 Compared with Vmax <5 m/s, patients with Vmax >/=5 m/s had greater mor

296 d significant excess mortality compared with Vmax 4 to 4.49 m/s (adjusted hazard ratio=1.34 [1.18-1.5

297 gen was measured as 11.2 +/- 0.5 microM with Vmax of 0.0041 +/- 0.0002 microM/(min.mg of hemoglobin).

298 readers 1 and 2, respectively), but not with Vmax (P = .13 and P = .21, readers 1 and 2, respectively

299 Compared with Vmax <5 m/s, patients with Vmax >/=5 m/s had greater mortality risk (adjusted hazar

300 tinocytes, 6(OH)M was the major product with Vmax = 63.7 ng/10(6) cells and Km = 10.2 muM, with lower