ライフサイエンスコーパス: Michaelis-Menten kinetics

1 sm by an approach similar to that used under Michaelis-Menten kinetics.

2 or substrates showed deviations from typical Michaelis-Menten kinetics.

3 e, and substrate concentration, and followed Michaelis-Menten kinetics.

4 cysteine uptake by transporters that exhibit Michaelis-Menten kinetics.

5 ision of 8-oxoG by OGG1 alone did not follow Michaelis-Menten kinetics.

6 Excision followed Michaelis-Menten kinetics.

7 induced caspase activation displayed typical Michaelis-Menten kinetics.

8 , and with the E2 isozyme, only neral obeyed Michaelis-Menten kinetics.

9 portional to enzyme concentration, and obeys Michaelis-Menten kinetics.

10 ixed Triton X-100 micelles follows classical Michaelis-Menten kinetics.

11 to unmodified PEPCK and demonstrates normal Michaelis-Menten kinetics.

12 ties are smaller than predicted from simple, Michaelis-Menten kinetics.

13 e-mediated renaturation of luciferase obeyed Michaelis-Menten kinetics.

14 High cholesterol content shifted E17betaG to Michaelis-Menten kinetics.

15 eir mean activity is consistent with classic Michaelis-Menten kinetics.

16 tions catalyzed by these nanorods follow the Michaelis-Menten kinetics.

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

18 response curve than that observed for simple Michaelis-Menten kinetics.

19 ere tested with respect to kinetic order and Michaelis-Menten kinetics.

20 her molecular weight oligomers and displayed Michaelis-Menten kinetics.

21 nover glycosylase assays are consistent with Michaelis-Menten kinetics.

22 -Trp oxidations (+/-cytochrome b(5)) exhibit Michaelis-Menten kinetics.

23 hydrolysis of various ceramides and followed Michaelis-Menten kinetics.

24 cs of the trimolecular system reduces to the Michaelis-Menten kinetics.

25 ar enzymatic system is more complex than the Michaelis-Menten kinetics.

26 rometry and were found to be consistent with Michaelis-Menten kinetics.

27 sis of both substrates could be described by Michaelis-Menten kinetics.

28 y DGAT1 does not behave according to classic Michaelis-Menten kinetics.

29 tion reaction, the adduct formation followed Michaelis-Menten kinetics.

30 for nitrite oxidation assuming one-component Michaelis-Menten kinetics.

31 nt, as measured on APM gels and evaluated by Michaelis-Menten kinetics.

32 estrogens to catechol estrogens according to Michaelis-Menten kinetics.

33 as substrates, the reaction followed normal Michaelis-Menten kinetics.

34 tal conditions for fitting the H-function to Michaelis-Menten kinetics.

35 the corresponding uncapped peptide displayed Michaelis-Menten kinetics.

36 PX activity indicating that the enzyme obeys Michaelis-Menten kinetics.

37 s a DNA-dependent ATPase that appears to fit Michaelis-Menten kinetics.

38 /electrocyclic ring opening obey saturation (Michaelis-Menten) kinetics.

39 The 1-268 fragment demonstrated Michaelis-Menten kinetics against ATP as substrate (Km 0

40 could substitute for glutamine and maintain Michaelis-Menten kinetics, albeit at a greatly reduced k

41 The enzyme exhibits classical Michaelis-Menten kinetics and acts cooperatively with a

42 or both enzymes were further analyzed using Michaelis-Menten kinetics and by structure probing.

43 ponding T. brucei flavoprotein (TbALO) obeys Michaelis-Menten kinetics and can utilize both L-galacto

44 n of the cGMP phosphodiesterase demonstrated Michaelis-Menten kinetics and competitive inhibition by

45 The C5 convertases appeared to follow Michaelis-Menten kinetics and exhibited similar catalyti

46 The catalysis reaction obeys Michaelis-Menten kinetics and exhibits competitive inhib

47 lucose transport process may be described by Michaelis-Menten kinetics and is analogous to recently d

48 et (Beta vulgaris) storage root approximates Michaelis-Menten kinetics and is strongly inhibited by a

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

50 is article, the well-established concepts of Michaelis-Menten kinetics and Langmuir binding isotherms

51 2-BBE cell monolayers displayed conventional Michaelis-Menten kinetics and was found to be pH-depende

52 evealed that the uptake followed first-order Michaelis-Menten kinetics and was high-affinity in natur

53 Clarithromycin transport exhibited Michaelis-Menten kinetics and was inhibited below 37 deg

54 NDC1 displayed Michaelis-Menten kinetics and was markedly inhibited by

55 quires zinc for catalytic activity, displays Michaelis-Menten kinetics, and is inhibited by S-adenosy

56 num site, the rate of NO production followed Michaelis-Menten kinetics, and oxygen functioned as a co

57 The purified enzyme obeyed normal Michaelis-Menten kinetics, and the K(m) for 5-hydroxyiso

58 bited both RT and RNase H activities, obeyed Michaelis-Menten kinetics, and was competitively inhibit

59 iple turnover) pyrophosphate exchange assay, Michaelis-Menten kinetics are observed.

60 analytical tools for enzymes displaying non-Michaelis-Menten kinetics are underdeveloped, and transi

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

62 ers (pH 7.5, 37 degreesC) WT Hsp104 exhibits Michaelis-Menten kinetics between 0.5 and 25 mM ATP (Km

63 This activity conformed to Michaelis-Menten kinetics but was unresponsive to substr

64 e sum of varying amounts of isoforms obeying Michaelis-Menten kinetics but with different values of K

65 "apparent" kinetic rate constants, based on Michaelis-Menten kinetics, can superficially show a depe

66 w the familiar Briggs-Haldane formulation of Michaelis-Menten kinetics derives from the outer (or qua

67 Michaelis-Menten kinetics emerge with reduction catalyze

68 obic XO-catalyzed nitrite reduction followed Michaelis-Menten kinetics, enabling prediction of the ma

69 We applied Michaelis-Menten kinetics featuring regulatory factors t

70 Reversible Michaelis-Menten kinetics fit these data best, and no di

71 cooperative kinetics for cis-retinoids, but Michaelis-Menten kinetics for 3alpha-hydroxysterols.

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

73 insights gleaned from linking Arrhenius and Michaelis-Menten kinetics for both photosynthesis and so

74 They obey Michaelis-Menten kinetics for hydrolysis of retinyl palm

75 Cytochrome P450 3A4 (CYP3A4) displays non-Michaelis-Menten kinetics for many of the substrates it

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

77 dies have indicated that CYP3A4 exhibits non-Michaelis-Menten kinetics for numerous substrates.

78 tic acid as substrates, the enzyme exhibited Michaelis-Menten kinetics; however, the enzyme did not u

79 The enzyme demonstrated Michaelis-Menten kinetics in an NADPH oxidation assay, b

80 gopeptidase), we unexpectedly discovered non-Michaelis-Menten kinetics in short time-scale measuremen

81 rative) behavior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent w

82 P2 substrates CCK8 and vasopressin exhibited Michaelis-Menten kinetics independent of membrane choles

83 PGE2/glutathione transport followed Michaelis-Menten kinetics irrespective of cholesterol.

84 wo most common BSEP variants p.444V/A showed Michaelis-Menten kinetics irrespective of membrane chole

85 Incision of alpha-C-Fapy.dA follows Michaelis-Menten kinetics (K(m) = 144.0 +/- 7.5 nM, k(ca

86 formed in the reaction which follows typical Michaelis-Menten kinetics (K(m) of 0.6 microM, and a V(m

87 The purified protein follows Michaelis-Menten kinetics (kcat = 5.7 s-1 and Km = 41 mi

88 coordinating picolinate ester 11, following Michaelis-Menten kinetics [kcat(11) = 2.3 min(-1) and Km

89 The reaction fits Michaelis-Menten kinetics (Km = 0.26 mM for ATP and 0.10

90 eine desulfhydrase resulted in the following Michaelis-Menten kinetics: Km = 3.6 mM and k(cat) = 12 s

91 thioxolone upon binding to CA II, including Michaelis-Menten kinetics of 4-nitrophenyl acetate ester

92 For comparison, we also measure the Michaelis-Menten kinetics of ADAMTS13 cleavage of wild-t

93 to account in interpreting the site-specific Michaelis-Menten kinetics of these reactions.

94 We exploited the abundance-dependent Michaelis-Menten kinetics of trypsin digestion to select

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

96 Michaelis-Menten kinetics permit estimates of maximal su

97 Michaelis-Menten kinetics provides a solid framework for

98 0F-P formation from phosphoramidate displays Michaelis-Menten kinetics, providing evidence for the pr

99 e basis of data modeling with simulations of Michaelis-Menten kinetics, rate maximum, V(max), varied

100 s demonstrated that biodegradation underwent Michaelis-Menten kinetics rather than first-order kineti

101 Michaelis-Menten kinetics revealed a Km of 169 mum and a

102 Michaelis-Menten kinetics studies revealed a classic non

103 Interestingly, Michaelis-Menten kinetics suggested that V477D had a 12-

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

105 ation of DA diffusion, including uptake with Michaelis-Menten kinetics, that provided estimates of DA

106 When the enzyme obeys Michaelis-Menten kinetics, the exact solution of the kin

107 Best described by Michaelis-Menten kinetics, the rate at which these varia

108 active near neutral pH (pH 7.0) and displays Michaelis-Menten kinetics toward the formylated dipeptid

109 s of AO-catalyzed nitrite reduction followed Michaelis-Menten kinetics under anaerobic conditions.

110 acidic pH optimum (4.5), and followed normal Michaelis-Menten kinetics using 14C- and BODIPY-labeled

111 igns were characterized in vitro in terms of Michaelis-Menten kinetics (V(MAX) and K(M)), sensitivity

112 A multispecies reactive transport model with Michaelis-Menten kinetics was developed to explain the c

113 OGG1 was increased approximately 5-fold and Michaelis-Menten kinetics were observed.

114 The reactions follow Michaelis-Menten kinetics where V(max) = 2420 +/- 490 mo

115 on of AC VI by Galpha(s) displayed classical Michaelis-Menten kinetics, whereas AC V activation by Ga

116 that long-chain (C14-C18) substrates follow Michaelis-Menten kinetics, whereas short and medium chai

117 The rate of nitrite production followed Michaelis-Menten kinetics, while NO generation rates inc

118 alpha13 abolishes cooperativity and restores Michaelis-Menten kinetics, while reducing the k(cat) val

119 the turnover signals were used to calculate Michaelis-Menten kinetics with a K(m) = 25 microM.

120 The reaction demonstrated Michaelis-Menten kinetics with a K(m) for oleoyl-CoA of

121 s active over a broad pH range and displayed Michaelis-Menten kinetics with a K(m) of 86 microm.

122 ecific protease was shown to exhibit typical Michaelis-Menten kinetics with a kcat of 0.086 +/- 0.002

123 active antibody, MATT.F-1, obeyed classical Michaelis-Menten kinetics with a Km = 104 microM, a kcat

124 *MtCM exhibits simple Michaelis-Menten kinetics with a Km of 0.5 +/- 0.05 mM a

125 The labeled RNA/DNA duplex demonstrated Michaelis-Menten kinetics with a Km value of 9.6+/-2.8 n

126 The rotation rates obeyed Michaelis-Menten kinetics with a maximal rotation rate (

127 e for the labelling could be described using Michaelis-Menten kinetics with an apparent KM of 40 micr

128 -hydroxysteroid dehydrogenase activity), but Michaelis-Menten kinetics with androsterone (3alpha-hydr

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

130 We described non-Michaelis-Menten kinetics with equations containing para

131 rolysis of the cocaine benzoyl ester follows Michaelis-Menten kinetics with k(cat) = 7.8 s(-1) and K(

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

133 The enzyme appears to follow Michaelis-Menten kinetics with Km for phosphoenolpyruvat

134 y aminoglycoside substrates while exhibiting Michaelis-Menten kinetics with others.

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

136 DGKA displayed Michaelis-Menten kinetics with respect to bulk substrate

137 The reaction exhibited Michaelis-Menten kinetics with respect to protoporphyrin

138 I-polyubiquitin chain assembly by hyperbolic Michaelis-Menten kinetics with respect to Ubc5B approxim

139 SPP1 exhibited apparent Michaelis-Menten kinetics with S1P as substrate with an

140 Both enzymes showed Michaelis-Menten kinetics with the K(m) lower for protei

141 nalization flux (Jint) followed first-order (Michaelis-Menten) kinetics with a calculated maximum int

142 xed micelles, the enzyme exhibited classical Michaelis-Menten kinetics, with a K(m) of 1.29 mol % and

143 ucleotide behaves like an enzyme and follows Michaelis-Menten kinetics, with a K(M) of 22 microM and

144 s were saturable and adequately described by Michaelis-Menten kinetics, with an apparent Km of 2.2+/-

145 supramolecular systems follow enzymatic-type Michaelis-Menten kinetics, with competitive product inhi

146 had a broad pH optimum of 6.6-7.5 and showed Michaelis-Menten kinetics, with Km values of 5 and 93 mi

147 n of the substrate by PTPN1 and PTPN2 obeyed Michaelis-Menten kinetics, with KM values of 770 +/- 250

148 eneralizations of the hyperbolic response of Michaelis-Menten kinetics x/(K+x), with fluctuating K or

149 Quantitation of the transfer rates by Michaelis-Menten kinetics yielded K(m) values of 6 and 0