Interfacial Tension of Hydrocarbon + Different pH Aqueous phase Systems in the Presence of Triton X-100

2010 ◽  
Vol 49 (7) ◽  
pp. 3228-3235 ◽  
Author(s):  
Javad Saien ◽  
Somayeh Akbari
2006 ◽  
Vol 27 (7) ◽  
pp. 927-930 ◽  
Author(s):  
Ke Ruan ◽  
Bao‐Huai Wang ◽  
Jin‐Xin Xiao ◽  
Jiao‐Ning Tang

1991 ◽  
Vol 280 (3) ◽  
pp. 745-751 ◽  
Author(s):  
N M Hooper ◽  
A Bashir

Treatment of kidney microvillar membranes with the non-ionic detergent Triton X-114 at 0 degrees C, followed by low-speed centrifugation, generated a detergent-insoluble pellet and a detergent-soluble supernatant. The supernatant was further fractionated by phase separation at 30 degrees C into a detergent-rich phase and a detergent-depleted or aqueous phase. Those ectoenzymes with a covalently attached glycosyl-phosphatidylinositol (G-PI) membrane anchor were recovered predominantly (greater than 73%) in the detergent-insoluble pellet. In contrast, those ectoenzymes anchored by a single membrane-spanning polypeptide were recovered predominantly (greater than 62%) in the detergent-rich phase. Removal of the hydrophobic membrane-anchoring domain from either class of ectoenzyme resulted in the proteins being recovered predominantly (greater than 70%) in the aqueous phase. This technique was also applied to other membrane types, including pig and human erythrocyte ghosts, where, in both cases, the G-PI-anchored acetylcholinesterase partitioned predominantly (greater than 69%) into the detergent-insoluble pellet. When the microvillar membranes were subjected only to differential solubilization with Triton X-114 at 0 degrees C, the G-PI-anchored ectoenzymes were recovered predominantly (greater than 63%) in the detergent-insoluble pellet, whereas the transmembrane-polypeptide-anchored ectoenzymes were recovered predominantly (greater than 95%) in the detergent-solubilized supernatant. Thus differential solubilization and temperature-induced phase separation in Triton X-114 distinguished between G-PI-anchored membrane proteins, transmembrane-polypeptide-anchored proteins and soluble, hydrophilic proteins. This technique may be more useful and reliable than susceptibility to release by phospholipases as a means of identifying a G-PI anchor on an unpurified membrane protein.


2016 ◽  
Vol 283 ◽  
pp. 251-259 ◽  
Author(s):  
Eva C. Sindermann ◽  
Alexander Holbach ◽  
André de Haan ◽  
Norbert Kockmann

1993 ◽  
Vol 290 (3) ◽  
pp. 791-795 ◽  
Author(s):  
L Klewes ◽  
E A Turley ◽  
P Prehm

The hyaluronate synthase complex was identified in plasma membranes from B6 cells. It contained two subunits of molecular masses 52 kDa and 60 kDa which bound the precursor UDP-GlcA in digitonin solution and partitioned into the aqueous phase, together with nascent hyaluronate upon Triton X-114 phase separation. The 52 kDa protein cross-reacted with poly- and monoclonal antibodies raised against the streptococcal hyaluronate synthase and the 60 kDa protein was recognized by monoclonal antibodies raised against a hyaluronate receptor. The 52 kDa protein was purified to homogeneity by affinity chromatography with monoclonal anti-hyaluronate synthase.


2018 ◽  
Vol 7 ◽  
pp. 133-142 ◽  
Author(s):  
Motasem Y.D. Alazaiza ◽  
Su Kong Ngien ◽  
Mustafa M. Bob ◽  
Samira A. Kamaruddin ◽  
Wan Mohd Faizal Ishak

2019 ◽  
Vol 56 (4) ◽  
pp. 1343-1351 ◽  
Author(s):  
Satoshi Sonobe ◽  
Yosuke Shibata ◽  
Naoya Minamishima ◽  
Yusuke Asakuma ◽  
Anita Hyde ◽  
...  

1992 ◽  
Vol 609 (1-2) ◽  
pp. 219-227 ◽  
Author(s):  
Harry Walter ◽  
Frank D. Raymond ◽  
Derek Fisher

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