1 the presence of 1 muM Cu(2+) at pH 6.0 (its
optimal pH).
2 ins abundant acid-sphingomyelinase activity (
optimal pH 5.1-5.6).
3 nique pH dependence for succinate transport (
optimal pH 7.5-8.5) and showed a high affinity for dimet
4 At the
optimal pH (
8.0), the kcat of MetAP1D of 0.39 min-1 is 2
5 The
optimal pH and activity profile obtained are in good agr
6 s known to form functional dodecamers at its
optimal pH and is thought to work in conjunction with an
7 The
optimal pH and temperature values of PKS11T161D were det
8 The
optimal pH and temperature were 8.0 and 50 degrees C, re
9 The
optimal pH and temperature were 9.0 and 50 degrees C, re
10 zyme L403R/G404R/A406S (K(m) values, V(max),
optimal pH and temperature) were essentially those of th
11 c properties, L-arginine kcat and Km values,
optimal pH,
and calmodulin binding affinity constant as
12 in terms of concentration of anion required,
optimal pH,
and incubation time needed.
13 t with Mg(2+) as an optimal metal ion and an
optimal pH around 5.
14 ceraldehyde-3-P dehydrogenases have the same
optimal pH as the enzyme isolated from pea chloroplasts.
15 substrate, the mutation led to a more basic
optimal pH as well as an increase in kcat and Km.
16 drugs across human epithelial cells requires
optimal pH-
dependent FcRn binding that can be manipulate
17 s have been systematically characterized for
optimal pH,
detergent, temperature, sonication, filtrati
18 n that in the bulk solution, creating a more
optimal pH environment for the anchored enzymes.
19 The
optimal pH for ACD activity was in the range of 7.0-9.0.
20 The
optimal pH for antibacterial activity against M. tubercu
21 key difference between the two complexes in
optimal pH for binding, as a result of differential pH-d
22 t the correct ring pucker is stable near the
optimal pH for both Cel6A and Cel7A.
23 at pH 7.0 are due to an upward shift in the
optimal pH for catalysis; a simple electrostatic model i
24 n at low ionic strength and pH 8.0, near the
optimal pH for enzymatic activity.
25 strate binding and catalysis and shifted the
optimal pH for enzyme activity further into alkaline sol
26 nents in the urine, the specificity, and the
optimal pH for galactokinase were studied.
27 of the chemiluminescence reaction as well as
optimal pH for light production.
28 The
optimal pH for mPrP(23-231) folding was found to be 4-5.
29 The
optimal pH for saposin B-mediated lipid binding to CD1d,
30 The
optimal pH for tetramer formation and reactivation is ab
31 The
optimal pH for the enzyme activity was 7.3.
32 The
optimal pH for the enzyme is 6.5.
33 The
optimal pH for the population of this state was found to
34 olecules, for example catecholamines, and an
optimal pH for the prohormone convertases which cleave h
35 In contrast, the
optimal pH for tryptase to cleave fibrinogen was acidic.
36 s applicable to enzymes with a wide range of
optimal pH,
from acid (pH 4.5) to alkaline phosphatase (
37 arsenate uptake capacity of 303 mg/g at the
optimal pH,
i.e., pH = 2.
38 Dried buffer components were used to set the
optimal pH in each detection reservoir, while precomplex
39 n vitro activity is Mg(2+)-dependent and its
optimal pH is 7.5, similar to that of Arabidopsis SFR2,
40 At the
optimal pH near 4.0, the preferred substrate is a 14-bas
41 At its
optimal pH of 4.0, the Michaelis-Menten parameters of K(
42 Since the enzyme showed an
optimal pH of 5.0, a value very similar to the one gener
43 that BDV G-mediated fusion takes place at an
optimal pH of 6.0 to 6.2, corresponding to an early-endo
44 for efficient pro-SRIF cleavage, even at the
optimal pH of 6.1.
45 rence for hydrophobic P2 residues, showed an
optimal pH of 6.7 in the presence of NaCl, demonstrated
46 At the
optimal pH of 7, the purified recombinant NUDT5 catalyze
47 ctivity was dependent upon magnesium with an
optimal pH of 7.5 and a native pI of 5.2.
48 Mg(2+)-dependent ATPase that functions at an
optimal pH of 7.5 and exhibits in vitro temperature depe
49 At an
optimal pH of 8.5, cooperative substrate activation by L
50 M) of 22 muM and 31 muM, respectively, under
optimal pH of 8.5-9.0 in a Ca(2+)-dependent manner.
51 alytic activities similar to NUDT5 under the
optimal pH of 9.
52 hree different peptide substrates and had an
optimal pH of approximately 7.5 and temperature optimum
53 nt with it being in the thiolate form at the
optimal pH of the enzyme.
54 At this
optimal pH,
preformed peroxidase-antiperoxidase immune c
55 The
optimal pH range for activation was 4.0 to 5.0, which in
56 The
optimal pH range for the nuclease activities of HEX1-N2
57 The
optimal pH range is approximately 7.0-8.1.
58 solute requirement for a divalent cation, an
optimal pH range of 7-8, and K(m) values of 124 micromet
59 = 15 +/- 2 microm) and carbon dioxide at an
optimal pH range of 7.0-7.5.
60 lute requirement for divalent cations and an
optimal pH range of 7.5 to 8.5, and the activity is stim
61 These pK(a)'s are in agreement with the
optimal pH range of the reaction and support the N-termi
62 The
optimal pH range was between pH 8.0 and 9.0.
63 The
optimal pH ranges for these two functions are also simil
64 rature from 45 to 55 degrees C, whereas, the
optimal pH remained same with reference to free enzyme.
65 d a small amount of enzyme activity with the
optimal pH shifted towards more acidic.
66 There is controversy regarding the
optimal pH strategy during deep hypothermic bypass in ch
67 Optimal pH,
temperature, and concentration of enzyme con
68 increased in magnitude upon changing from an
optimal pH to a nonoptimal pH; the 18(V/K)bridge effect
69 Optimal pH to stabilize TPs in SMT was ca. 5.7, which re
70 An
optimal pH value of 8.5 was obtained under these conditi
71 The
optimal pH value was determined as 3.
72 Optimal pH values vary from 6.8 for caspase-8 to 7.4 for
73 The
optimal pH values were 5.5 for catechol and 4-methylcate
74 With pro-TNFalpha the
optimal pH was approximately 7.4, whereas with the pepti
75 7.4, whereas with the peptide substrate the
optimal pH was higher than 9.0.
76 This
optimal pH was verified through underwater wetting behav
77 fer to O(2) of lambda = 28 kcal mol(-)(1) at
optimal pH,
which is similar to the value obtained earli