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

1 substrate concentrations greatly exceeds the Michaelis-Menten constant.

2 ity as expected, but also raise the apparent Michaelis-Menten constant.

3 determine the maximal turnover rate and the Michaelis-Menten constant.

4 , optimal enzymatic reaction conditions, and Michaelis-Menten constants.

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

6 1.8x10(-9) mol/cm(2)) and the small value of Michaelis-Menten constant (0.76 mM) confirmed an excelle

7 se stimulation experiments show that the net Michaelis-Menten constant (6.1+/-1.5 mM) is in between G

8 posite was revealed by the high value of the Michaelis-Menten constant (79.3 muM).

9 ells demonstrated a 2.2-fold increase in the Michaelis-Menten constant, a 2.5-fold increase in the ap

10 d for the inward transport with the apparent Michaelis-Menten constant and a maximum transport rate o

11 Go6976 progressively increased the Michaelis-Menten constant and decreased the Hill coeffic

12 osphatase rates and/or by sufficiently large Michaelis-Menten constants and sufficiently low amounts

13 -substrate complexes dissociation constants (Michaelis-Menten constants) and by the reorganization en

14 a combination of microscopic reaction rates, Michaelis-Menten constants, and biochemical concentratio

15 meters, such as decay rates, reaction rates, Michaelis-Menten constants, and Hill coefficients.

16 ies (genus Sphyraena) display differences in Michaelis-Menten constants (apparent Km) for substrate (

17 the transport of citrate with high affinity (Michaelis-Menten constant, approximately 20 microm) and

18 From these results, apparent Michaelis-Menten constants as well as the kinetic parame

19 ent pH optima ranged from pH 5.4 to 6.4 with Michaelis-Menten constants between 0.84 +/- 0.09 and 4.6

20 The Michaelis Menten constant calculated from the linear por

21 immobilization, with values of the apparent Michaelis-Menten constants estimated as 7.71 +/- 0.62 an

22 .g. degradation rate, production rate, Kcat, Michaelis-Menten constant, etc.) and the initial concent

23 The Michaelis-Menten constant for InsP(5) was 0.4 microM and

24 ts of the temperature dependency of the PEPc Michaelis-Menten constant for its substrate HCO3 (-), an

25 of the nascent RNA and reduces the apparent Michaelis-Menten constant for nucleotides, suggesting th

26 uring SNARE-stimulated ATP hydrolysis rates, Michaelis-Menten constants for disassembly, and SNAP-SNA

27 Moreover, the constraints do not require Michaelis-Menten constants for most enzymes, and they on

28 he binding constants are similar, as are the Michaelis-Menten constants for substrate hydrolysis.

29 Determination of Michaelis-Menten constants for the substrates with Ultra

30 at natural selection may have fine-tuned the Michaelis-Menten constant [Formula: see text] describing

31 +/- 0.9 min(-1), P < 0.05) and increased the Michaelis-Menten constant K(M) (204 +/- 6 n(M) to 478 +/

32 maximal velocities V(max) and the effective Michaelis-Menten constants K(M) under physiologically re

33 Recently it was reported that Michaelis Menten constants (K(m)) of oxidative enzymes a

34 cles, Nafion(R) and glucose oxidase (GOx), a Michaelis-Menten constant (K'(m)) of 20-30 mM is obtaine

35 orable binding of the probe with TrxR with a Michaelis-Menten constant (K(m) ) of 15.89 mum.

36 110 +/- 1.3 nA/(mM mm(2)) with the apparent Michaelis-Menten constant (K(M)(app)) derived from an L-

37 The apparent Michaelis-Menten constant (K(M)(app)) of HRP on the nano

38 Factor XI-R226 activates factor IX with a Michaelis-Menten constant (K(m)) about 5-fold greater th

39 The apparent Michaelis-Menten constant (K(m)) and Hb adsorption in th

40 The Michaelis-Menten constant (k(m)) and turnover number (k(

41 The low value of 0.13 x 10(-4) M of Michaelis-Menten constant (K(m)) indicate the enhanced a

42 lfonic acid)-diammonium salt (ABTS) with the Michaelis-Menten constant (K(M)) of 0.018 mM in a test f

43 A low Michaelis-Menten constant (K(m)) of 0.12 mM, indicate th

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

45 We quantified (i) apparent Michaelis-Menten constant (K(m)) of fructose 6-phosphate

46 t (K(i)) values similar to or lower than the Michaelis-Menten constant (K(m)) values of ATP.

47 The Michaelis-Menten constant (K(m)) was determined as 3.3 m

48 al enzymatic conversion rate (A(max)) to the Michaelis-Menten constant (K(m)), i.e., A(max)/K(m), bef

49 The Michaelis-Menten constant (K(m)), the maximum velocity (

50 ocity (V(max)) without significant change in Michaelis-Menten constant (K(m)).

51 x)) without any modification in the apparent Michaelis-Menten constant (K(m)).

52 Factor Xa generation assays showed similar Michaelis-Menten constant (K(m), apparent) values for th

53 The low value of the Michaelis-Menten constant (K(m)=0.34 mM) indicates the h

54 clability, storage stability, precision, and Michaelis-Menten constants (K(m)) for ATP and d-luciferi

55 d 3,3',5,5'- tetramethylbenzidine (TMB) with Michaelis-Menten constants (K(M)) of 0.1301 and 0.0141 m

56 The corresponding Michaelis-Menten constants (K(m)) were 1.9 microM and 20

57 nsported by OATP1A2 and OATP1A5 with similar Michaelis-Menten constants (K(m)).

58 ics revealed that C-1-P had no effect on the Michaelis-Menten constant, K(m)(B), but decreased the di

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

60 The Michaelis-Menten constant Km values are 2.0 microM for m

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

62 The apparent Michaelis-Menten constant (KM(app)) was calculated to be

63 The apparent Michaelis-Menten constant (Km(app)) was calculated to be

64 The observed Michaelis-Menten constant (Km) and catalytic constant (K

65 The Michaelis-Menten constant (Km) and catalytic constant (k

66 Purified lipase had Michaelis-Menten constant (Km) and catalytic constant (k

67 05M mutant of 3beta-HSD1 (Q105M1) shifts the Michaelis-Menten constant (Km) for 3beta-HSD substrate a

68 related with substrate concentration, with a Michaelis-Menten constant (Km) of 0.3 +/- 0.03 mM and a

69 was evaluated and found to have an apparent Michaelis-Menten constant (KM) of 1.2 mM for the indolyl

70 cine was time dependent and saturable with a Michaelis-Menten constant (Km) of 27+/-3 microM.

71 nd respiratory proton currents, estimate the Michaelis-Menten constant (Km) of PR (10(3) photons per

72 2O2 with a detection limit of 0.48microM and Michaelis-Menten constant (Km) value of 44.2microM.

73 The Michaelis-Menten constant (Km) value of Hb at the modifi

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

75 A lower value of Michaelis-Menten constant (Km), of 0.062 mM for the cova

76 The low value of the Michaelis-Menten constant (Km=0.47 mM) indicates the hig

77 Higher Michaelis-Menten constants (Km) and catalytic rate const

78 This enables rapid quantification of Michaelis-Menten constants (KM) for different substrates

79 The observed Michaelis-Menten constants (KM) for factor VII activatio

80 The apparent Michaelis-Menten constants (KM) for MBP-NR in solution a

81 min(-1), respectively, and the corresponding Michaelis-Menten constants (Km) were 10 and 8 microm.

82 tively, and the values for the corresponding Michaelis-Menten constants (Km) were 280, 160, and 16 mi

83 cm(-2) for the urea biosensor, with apparent Michaelis-Menten constants (KM,app), obtained from the c

84 ses showed that alpha KG reduction (apparent Michaelis-Menten constant [Km(app)] = 88 microM; apparen

85 The Michaelis-Menten constant, KM , for PO4 remained constan

86 these experiments with previously determined Michaelis-Menten constants (Kms) for the enzyme activity

87 The Michaelis-Menten constant (Kt) for the transport of pant

88 ccurred by a single saturable process with a Michaelis-Menten constant of 0.13 +/- 0.01 microM.

89 pendency over 0.02 to 10 mM with an apparent Michaelis-Menten constant of 3.1 mM and a maximal flux o

90 The apparent Michaelis-Menten constant of Hb on the PpPDA@Fe3O4 nanoc

91 yosin, though the Km(app) (apparent (fitted) Michaelis-Menten constant) of F-actin speed with ATP tit

92 ons of substrates and cofactors and apparent Michaelis-Menten constants, suggesting that the two para

93 he use of acetate buffers resulted in larger Michaelis-Menten constants, up to 14.62 +/- 2.03 mM.

94 ng peroxidase-like activity, achieving a low Michaelis-Menten constant using 3,3',5,5'-tetramethylben

95 The Michaelis-Menten constants Vmax, KM, and kcat of Atm1-C

96 For the saturable process, the apparent Michaelis-Menten constant was 1.9 mM, the maximum flux w

97 Maximal clearance was 7.25 L/h, and the Michaelis-Menten constant was 27.2 mg/L.

98 However, Michaelis-Menten constant was significantly increased at

99 that the immobilization process changed the Michaelis-Menten constant, which means that the substrat