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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 ophotrochozoan nACh-like receptor in which a CHAPS molecule is tightly bound to the orthosteric site.
7 pyl)dimethylammonio]-1-propanesulfonic acid (CHAPS) is unique in its ability to stabilize the recepto
8 ylammonio]-2-hydroxy-1-propanesulfonic acid (CHAPS), 10% sucrose, pH 7.2.
9 yl)-dimethylammonio]-1-propanesulfonic acid (CHAPS)-solubilized fraction and eluted with peptide epit
10 yl)dimethylammonio]-1-propanesulfonic acid] (CHAPS) also lowers (1-->3),(1-->4)-beta-glucan synthase
11                                        After CHAPS solubilization of Chinese Hamster Ovary cells, the
12 ure to mild neutral detergents (Tween 20 and CHAPS) at concentrations from 0.25 to 2.0%.
13  remained largely intact and sedimentable at CHAPS concentrations (4%) where >90% of the phospholipid
14 1 in the presence of the detergent deoxy big CHAPS, and determined its structure at 1.8 A resolution
15 ta40 levels was seen at 12 mo of age in both CHAPS-soluble and formic acid (FA)-soluble brain fractio
16 g proteins followed by displacement of GR by CHAPS.
17 uced destabilization of membrane proteins by CHAPS or digitonin.
18 nal fold of CB(2) in dodecyl maltoside (DDM)/CHAPS detergent solutions.
19 dodecyltrimethylammonium chloride, and a DDM/CHAPS/CHS mixture.
20 een 20, sodium cholate, sodium deoxycholate, CHAPS, or CHAPSO, are completely ineffective COX solubil
21                 This preparation, designated CHAPS-insoluble floating fraction (CHIEF), also containe
22 omatography in the presence of the detergent CHAPS (3-[(3-cholamidopropyl)-dimethylammonio]-1-propane
23 s from B. subtilis, as well as the detergent CHAPS, when combined with C12EO8.
24 to extraction by the zwitterionic detergent, CHAPS.
25 ring the differential effects of detergents (CHAPS vs octyl glucoside), we have shown that this direc
26 cillus subtilis QST713 as well as digitonin, CHAPS, and lysophosphatidylcholine solubilize membranes
27 ne apoprotein intermediate state in SDS/DMPC/CHAPS micelles.
28  with Golgi membranes at synthesis-enhancing CHAPS concentrations but lost if the CHAPS-soluble fract
29  CHAPS-soluble fraction is replaced by fresh CHAPS buffer.
30 ose, S-thiolated proteins were purified from CHAPS-soluble kidney homogenate.
31                       Some detergents (e.g., CHAPS and dodecyl maltoside) promote the dissociation of
32 dimethylammonio]-1-propanesulfonate hydrate (CHAPS) micelle of total molecular mass approximately 45-
33 CD36 from platelets that were solubilized in CHAPS and Brij 99 but not from platelets that were solub
34 ase (PPEP) activity, has been solubilized in CHAPS and purified 5-fold.
35                               Interestingly, CHAPS and Triton X-100, thanks to similar surface bindin
36 ds were solubilized using 8 m urea and 10 mm CHAPS.
37                  We show that the binding of CHAPS leads to extending of the loop C at the orthosteri
38 tion highly enriched in cAR1 by flotation of CHAPS lysates of cells in sucrose density gradients.
39 HisACAT-1 with the detergent deoxycholate or CHAPS (3-[(3-cholamidopropyl)-dimethylammonio]-1-propane
40 .g., sodium cholate, sodium deoxycholate, or CHAPS.
41 opropyl)dimethylammonio]-1-propanesulfonate (CHAPS) as a matrix modifier is introduced as a novel app
42 ropyl)-dimethyl-ammonio]-1-propanesulfonate (CHAPS) extraction and characterized with regard to exope
43 opyl)- dimethyl-ammoniol-1-propanesulfonate (CHAPS) inhibited protease activity at a concentration of
44 opropyl)dimethylammonio]-1-propanesulfonate (CHAPS), 3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy
45 opropyl)dimethylammonio]-1-propanesulfonate (CHAPS), Brij 96, or Brij 99, and the proteins that copre
46 propyl)dimethyl-ammonio]-1-propanesulfonate (CHAPS), micelles contain mostly dimeric Rho.
47 opropyl)dimethylammonio]-1-propanesulfonate (CHAPS), which increased FM1-43 quantum yield by more tha
48 propyl) dimethylammonio]-1-propanesulfonate (CHAPS, zwitterionic), Triton X-100 (nonionic), sodium do
49 idopropyl)dimethylammonio]-propanesulfonate (CHAPS), the M formation and decay kinetics are much slow
50 opropyl)dimethylammonio]-1-propanesulfonate [CHAPS], octylglucoside) extraction, suggesting that M1 a
51                                  It requires CHAPS detergent and Mg(2+) for activity.
52 opropyl)dimethylammonio-1-propane sulfonate (CHAPS)/SDS and l-alpha-1,2-dihexanoylphosphatidylcholine
53 hancing CHAPS concentrations but lost if the CHAPS-soluble fraction is replaced by fresh CHAPS buffer
54 agilis ATCC 25285(pFD340-prtP) cells nor the CHAPS extract effected hemagglutination of sheep red blo
55   The Gbetagamma-mediated binding of GRK2 to CHAPS micelles or lipid bilayers therefore appears to ri
56 ranes or Triton X-100 extracts, assays using CHAPS- or tDOC-washed membranes were found to be reprodu
57 uced in Sf9 cells could be solubilized using CHAPS in a form capable of binding erythropoietin, and t
58 rs for the two IPC synthase substrates using CHAPS-washed membranes resulted in K(m) values of 3.3 an