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

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

5 1.8x10(-9) mol/cm(2)) and the small value of Michaelis-Menten constant (0.76 mM) confirmed an excelle

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

25 110 +/- 1.3 nA/(mM mm(2)) with the apparent Michaelis-Menten constant (K(M)(app)) derived from an L-

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

49 05M mutant of 3beta-HSD1 (Q105M1) shifts the Michaelis-Menten constant (Km) for 3beta-HSD substrate a

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

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

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

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

54 2O2 with a detection limit of 0.48microM and Michaelis-Menten constant (Km) value of 44.2microM.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

78 However, Michaelis-Menten constant was significantly increased at