ライフサイエンスコーパス: CHAPS

1 CHAPS-solubilized recombinant ACS6 protein preferred uti

2 wild-type AQP2 was >95% solubilized by 0.5% CHAPS whereas T126M was <10% solubilized.

3 At 2.5% CHAPS, a concentration where approximately 50% of the pr

4 olubilized using detergent conditions (0.75% CHAPS, 1 mg/ml phosphatidylcholine) predicted to retain

5 f the cellotriosyl units is recovered when a CHAPS-soluble factor is permitted to associate with Golg

6 pyl)dimethylammonio]-1-propanesulfonic acid (CHAPS) is unique in its ability to stabilize the recepto

7 ylammonio]-2-hydroxy-1-propanesulfonic acid (CHAPS), 10% sucrose, pH 7.2.

8 yl)-dimethylammonio]-1-propanesulfonic acid (CHAPS)-solubilized fraction and eluted with peptide epit

9 yl)dimethylammonio]-1-propanesulfonic acid] (CHAPS) also lowers (1-->3),(1-->4)-beta-glucan synthase

10 After CHAPS solubilization of Chinese Hamster Ovary cells, the

11 ure to mild neutral detergents (Tween 20 and CHAPS) at concentrations from 0.25 to 2.0%.

12 remained largely intact and sedimentable at CHAPS concentrations (4%) where >90% of the phospholipid

13 1 in the presence of the detergent deoxy big CHAPS, and determined its structure at 1.8 A resolution

14 ta40 levels was seen at 12 mo of age in both CHAPS-soluble and formic acid (FA)-soluble brain fractio

15 g proteins followed by displacement of GR by CHAPS.

16 uced destabilization of membrane proteins by CHAPS or digitonin.

17 nal fold of CB(2) in dodecyl maltoside (DDM)/CHAPS detergent solutions.

18 dodecyltrimethylammonium chloride, and a DDM/CHAPS/CHS mixture.

19 een 20, sodium cholate, sodium deoxycholate, CHAPS, or CHAPSO, are completely ineffective COX solubil

20 This preparation, designated CHAPS-insoluble floating fraction (CHIEF), also containe

21 omatography in the presence of the detergent CHAPS (3-[(3-cholamidopropyl)-dimethylammonio]-1-propane

22 s from B. subtilis, as well as the detergent CHAPS, when combined with C12EO8.

23 to extraction by the zwitterionic detergent, CHAPS.

24 ring the differential effects of detergents (CHAPS vs octyl glucoside), we have shown that this direc

25 cillus subtilis QST713 as well as digitonin, CHAPS, and lysophosphatidylcholine solubilize membranes

26 ne apoprotein intermediate state in SDS/DMPC/CHAPS micelles.

27 with Golgi membranes at synthesis-enhancing CHAPS concentrations but lost if the CHAPS-soluble fract

28 CHAPS-soluble fraction is replaced by fresh CHAPS buffer.

29 ose, S-thiolated proteins were purified from CHAPS-soluble kidney homogenate.

30 Some detergents (e.g., CHAPS and dodecyl maltoside) promote the dissociation of

31 dimethylammonio]-1-propanesulfonate hydrate (CHAPS) micelle of total molecular mass approximately 45-

32 CD36 from platelets that were solubilized in CHAPS and Brij 99 but not from platelets that were solub

33 ase (PPEP) activity, has been solubilized in CHAPS and purified 5-fold.

34 Interestingly, CHAPS and Triton X-100, thanks to similar surface bindin

35 ds were solubilized using 8 m urea and 10 mm CHAPS.

36 tion highly enriched in cAR1 by flotation of CHAPS lysates of cells in sucrose density gradients.

37 HisACAT-1 with the detergent deoxycholate or CHAPS (3-[(3-cholamidopropyl)-dimethylammonio]-1-propane

38 .g., sodium cholate, sodium deoxycholate, or CHAPS.

39 opropyl)dimethylammonio]-1-propanesulfonate (CHAPS) as a matrix modifier is introduced as a novel app

40 ropyl)-dimethyl-ammonio]-1-propanesulfonate (CHAPS) extraction and characterized with regard to exope

41 opyl)- dimethyl-ammoniol-1-propanesulfonate (CHAPS) inhibited protease activity at a concentration of

42 opropyl)dimethylammonio]-1-propanesulfonate (CHAPS), 3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy

43 opropyl)dimethylammonio]-1-propanesulfonate (CHAPS), Brij 96, or Brij 99, and the proteins that copre

44 propyl)dimethyl-ammonio]-1-propanesulfonate (CHAPS), micelles contain mostly dimeric Rho.

45 opropyl)dimethylammonio]-1-propanesulfonate (CHAPS), which increased FM1-43 quantum yield by more tha

46 propyl) dimethylammonio]-1-propanesulfonate (CHAPS, zwitterionic), Triton X-100 (nonionic), sodium do

47 idopropyl)dimethylammonio]-propanesulfonate (CHAPS), the M formation and decay kinetics are much slow

48 opropyl)dimethylammonio]-1-propanesulfonate [CHAPS], octylglucoside) extraction, suggesting that M1 a

49 It requires CHAPS detergent and Mg(2+) for activity.

50 opropyl)dimethylammonio-1-propane sulfonate (CHAPS)/SDS and l-alpha-1,2-dihexanoylphosphatidylcholine

51 hancing CHAPS concentrations but lost if the CHAPS-soluble fraction is replaced by fresh CHAPS buffer

52 agilis ATCC 25285(pFD340-prtP) cells nor the CHAPS extract effected hemagglutination of sheep red blo

53 The Gbetagamma-mediated binding of GRK2 to CHAPS micelles or lipid bilayers therefore appears to ri

54 ranes or Triton X-100 extracts, assays using CHAPS- or tDOC-washed membranes were found to be reprodu

55 uced in Sf9 cells could be solubilized using CHAPS in a form capable of binding erythropoietin, and t

56 rs for the two IPC synthase substrates using CHAPS-washed membranes resulted in K(m) values of 3.3 an