ライフサイエンスコーパス: Tween 20

1 ta-lactoglobulin) or a non-ionic surfactant (Tween 20).

2 le to colour fading than those stabilized by Tween 20.

3 eased when the enzyme assays contained 0.02% Tween 20.

4 molecular-weight oligomers are stabilized by Tween 20.

5 formulations containing sucrose, salts, and Tween 20.

6 the growth of 8830R2::Cm in the presence of Tween 20.

7 n X-100 (RTX-100), octylglucopyranoside, and Tween 20.

8 led these strains to grow in the presence of Tween 20.

9 wells; unbound AFP was then washed away with Tween-20.

10 nt of black currants with 0.02mM MJ in 0.05% Tween-20.

11 ly, when the assay buffer contains traces of Tween 20 (0.0001%), darbufelone appears inactive with PG

12 sence of low concentrations of the detergent Tween 20 (0.05-0.1%, v/v) in the wash buffer as well as

13 glucoside, dodecyl maltoside, Triton X-100, Tween 20, 3-[(3-cholamidopropyl)dimethylammonio]-1-propa

14 For steric emulsifiers, Tween 20, 40, 60 and 80 were used to produce nanodispers

15 factant-to-oil ratio (SOR), surfactant type (Tween 20, 40, 60, 80 and 85), and stirring conditions on

16 d to study the influence of surfactant type (Tween 20, 60 and 80) and oil type (Vitamin E, vitamin D(

17 a major impact of non-ionic surfactant type (Tween 20, 60 or 80) on the formation and properties of t

18 in their ability to grow in the presence of Tween 20, a detergent that inhibits a kinase which can s

19 ied starch and whey protein isolate, but not Tween 20, affected the cell viability/proliferation more

20 1 hour) and chemical inactivation with 0.5% Tween-20 against a high titer of Ebola virus (species Za

21 The Tween 20 allowed lower detection limits to be obtained f

22 formulations with aqueous solutions of 0.03% Tween 20 altered the time of dissolution for all cases.

23 m the Schirmer strip in 0.5 M NaCl with 0.5% Tween 20 and analyzed using multiplex assay kits to exam

24 pted by exposure to mild neutral detergents (Tween 20 and CHAPS) at concentrations from 0.25 to 2.0%.

25 mines the potential of two buffer additives (Tween 20 and DTT) to improve the solubility of proteins

26 formation is inhibited by concentrations of Tween 20 and several other detergents well below their c

27 nanoemulsions emulsified by modified starch, Tween 20 and whey protein isolate, respectively, were pr

28 Three types of emulsifiers, lecithin, Tween-20 and sodium dodecyl sulphate (SDS) were tested.

29 a, Polyethylene glycol sorbitan monolaurate (Tween 20) and Cetylpyridinium chloride (CPC) in Tris/HCl

30 was observed in W-1, Chaps, octyl glucoside, Tween 20, and Brij 35.

31 ol, W-1, octyl glucoside, dodecyl maltoside, Tween 20, and sodium cholate allow varying degrees of Ba

32 on of nonionic surfactants (Triton X-100 and Tween 20) arrays from the second series exhibit signific

33 m) were formed using a non-ionic surfactant (Tween 20) as emulsifier and long chain triglycerides (LC

34 hed three times, then solubilized with 0.04% Tween 20 at a detergent/protein (w/w) ratio of 0.1.

35 A tween 20 coating method is developed to inhibit non-spec

36 gents such as Triton X-100, Nonidet P-40 and Tween 20 did not affect the activities, while anionic de

37 In contrast, formulations containing Tween 20 dissolved faster in the Tween 20 solution when

38 Salt and sucrose formulations without Tween 20 dissolved more slowly in a Tween 20 solution th

39 method based on dichlorodimethylsilane (DDS)-Tween-20 for in vitro single-molecule studies, which, un

40 rol (0.5% carboxymethyl cellulose and 0.025% Tween 20 in distilled water) or 750 mg silibinin/kg body

41 affect darbufelone in this way, in place of Tween 20 in our PGHS buffers.

42 containing 0.5% methyl cellulose and 0.025% Tween 20 in two different protocols.

43 were prepared from mixtures of olive oil and Tween 20 in water.

44 ates, in emulsions prepared with lecithin or Tween-20, indicating the greater relevance of having thr

45 ic acid and autoxidation of linoleic acid in Tween 20 micellar medium) and compared with three widely

46 However, Tween 20 micelles did appear to be able to solubilise le

47 E(8), followed by exchange of C(12)E(8) with Tween 20 on a Superose 6 column.

48 thesis could be abolished by the addition of Tween 20 or Triton X-100.

49 ions, from the nonionic class (Triton X-100, Tween 20) or from the zwitterionic class (3-[(3-cholamid

50 Moreover, the influence of Tween 20 over the analytical parameters was studied.

51 r and StartingBlock phosphate buffer saline- Tween-20; (PBS-T20) blocking buffer was utilized to mini

52 e substrate in 50 mM NaOAc, 150 mM KF, 0.05% Tween 20, pH 5.5, with apparent first-order kinetics wit

53 which neutral additives (e.g., Triton X-100, Tween 20, poly(ethylene glycol)) are removed from protei

54 Dilution experiments of cinaciguat/Tween 20-preincubated sGC revealed the irreversible char

55 nd poorly to MTP, but its preincubation with Tween-20 resulted in significantly increased binding to

56 riments with purified sGC in the presence of Tween 20 showed that cinaciguat activates the heme-free

57 Other detergents, e.g., Tween 20, sodium cholate, sodium deoxycholate, CHAPS, or

58 y bound cardiolipin (CL) can be removed from Tween 20 solubilized bovine cytochrome bc(1) (EC 1.10.2.

59 Phospholipid removal from the Tween 20 solubilized enzyme, including the tightly bound

60 without Tween 20 dissolved more slowly in a Tween 20 solution than in water alone.

61 containing Tween 20 dissolved faster in the Tween 20 solution when compared to dissolution in water.

62 ctoglobulin-stabilised nanoemulsions than in Tween 20-stabilised ones.

63 Tween 20 stabilized corn O/W emulsions at pH 7.0 were pr

64 d autoxidation within single oil droplets in Tween-20-stabilized oil-in-water emulsion was achieved b

65 Lastly, Tween 20 substantially and selectively increases NTPDase

66 The DDS-Tween-20 surface was simple and inexpensive to prepare a

67 In contrast, for emulsions prepared with Tween-20, the antioxidants seem to follow the polar para

68 a Tris-HCl buffer containing the surfactant Tween 20 to aid in the prevention of surface adhesion of

69 ngth of the desalted serum and also utilized Tween 20 to serve as the passivation agent by surface mo

70 ution (1.5% carboxymethylcellulose with 0.2% Tween 20) via gastrointestinal gavage.

71 The detergent polysorbate 20 (Tween 20) was used successfully to facilitate the remova

72 ulsions consisting of water, tricaprylin and Tween 20 were prepared, thermally treated and the format