Disease relevance of EINECS 225-856-4

• The di-tripeptide transport system (DtpT) of Lactococcus lactis was purified to apparent homogeneity by pre-extraction of crude membrane vesicles with octaethylene glycol monodecyl ether (C10E8), followed by solubilization with n-dodecyl-beta-D-maltoside (DDM) and chromatography on a Ni-NTA resin [1].

High impact information on EINECS 225-856-4

• The oligomeric state of newly synthesized band 3 in early and late erythroblasts was analyzed by size-exclusion high-pressure liquid chromatography of band 3 extracts derived by mild extraction of plasma membranes with the nonionic detergent C12E8 (octaethylene glycol n-dodecyl monoether) [2].
• The antisera in competitive enzyme-linked immunosorbent assays only reacted with intact SR vesicles to a limited extent, but most epitopic regions were exposed by low concentrations of nondenaturing detergent, octaethylene glycol dodecyl ether (C12E8) or after removal of cytosolic regions by proteinase K [3].
• Size-exclusion chromatography in the presence of octaethylene glycol monododecyl ether indicated that the solubilized yeast-expressed AE1, like endogenous erythroid AE1, eluted at a stokes radius of 77 A, consistent with a dimeric oligomeric state [4].
• The oligomeric state of human Band 3 (Mr = 95,000), the erythrocyte membrane anion exchanger, was examined by size exclusion high performance liquid chromatography in solutions containing the nonionic detergent C12E8 (octaethylene glycol n-dodecyl monoether) [5].
• With nonsolubilizing concentrations of the nonionic detergent, octaethylene glycol monododecyl ether, the hydrolysis of GTP was rendered partially calcium-sensitive resulting from a slightly increased total (Ca2+ + Mg2+)-GTPase activity and a markedly inhibited calcium-independent (Mg2+-dependent) GTPase activity [6].

Biological context of EINECS 225-856-4

• The present pendant-drop model is applied to study the adsorption kinetics of surfactant C10E8 (octaethylene glycol mono n-decyl ether) at the water-air interface of a pendant drop [7].

Anatomical context of EINECS 225-856-4

• The mechanism of ATP hydrolysis was studied at 0 degrees C and pH 7.5 using purified leaky vesicles of sarcoplasmic reticulum Ca2+-ATPase and enzyme solubilized in monomeric form with high concentrations of octaethylene glycol monododecyl ether (C12E8) [8].
• We previously characterized the structural features of the interaction of sarcoplasmic reticulum membranes with nonsolubilizing concentrations of C12E8, the non-ionic detergent octaethylene glycol monododecyl ether (Andersen, J.P., le Maire, M., Kragh-Hansen, V., Champeil, P., and Møller, J. V. (1983) Eur. J. Biochem. 134, 205-214) [9].
• We investigated the effects of the nonionic detergent octaethylene glycol monododecyl ether (C12E8) on the sarcoplasmic reticulum calcium pump in cardiac microsomes in view of its specific effects on different ATP-accelerated steps in the catalytic cycle of the Ca-ATPase in leaky fast skeletal muscle microsomes [10].
• High- and low-affinity Na(+)-dependent neutral L-alpha-amino acid transporters were solubilized with 0.25% octaethylene glycol dodecyl ether (C12E8) after removal of the proteins from the brush-border membrane vesicles with 2% CHAPS and 4 M urea [11].

Associations of EINECS 225-856-4 with other chemical compounds

• An alternate purification method was then developed, based on solubilization of SRV with dodecyl octaethylene glycol monoether ( C12E8 ), separation of delipidated ATPase by anion-exchange chromatography, and enzyme reactivation with phosphatidylcholine [12].
• We also discuss results for rhodopsin solubilized in a nonionic detergent (octaethylene glycol n-dodecyl ether) in which the detergent is clearly causing irreversible loss of the capability to recombine with 11-cis-retinal [13].
• Phospholipid-free rhodopsin has been purified in the detergents sodium cholate and octaethylene glycol n-dodecyl ether (C12E8) [14].
• External reflection Fourier transform infrared spectroscopy (ERFTIRS) has been used to obtain spectra of monolayers of the hydrocarbon surfactant octaethylene glycol monodecyl ether (C(10)E(8)) and the fluorocarbon surfactant ammonium perfluorononanoate (APFN) at the expanding liquid surface of an overflowing cylinder [15].
• The Ca(2+)-ATPase expressed in light membranes was 100% solubilized with L-alpha-lysophosphatidylcholine (LPC), 50% with n-dodecyl beta-D-maltoside (DM) and 25% with octaethylene glycol mono-n-dodecyl ether (C(12)E(8)) [16].

Gene context of EINECS 225-856-4

• Treatment of nb/nb ghosts with the nonionic detergent C12E8 (octaethylene glycol n-dodecyl monoether) resulted in nearly complete extraction of band 3 [17].
• In this approach, we used a running electrolyte containing 3 x 10(-2) mol/L H3PO4 electrolyte (pH 2.5) and octaethylene glycol monododecyl ether (C12E8) as neutral surfactant [18].
• A fraction containing cytochrome c1 was then eluted with buffer containing 1% dodecyl octaethylene glycol monoether [19].
• An octaethylene glycol monododecyl ether-based mixed micellar assay for determining the lipid acyl hydrolase activity of patatin [20].

Analytical, diagnostic and therapeutic context of EINECS 225-856-4

• Sarcoplasmic reticulum Ca2+-ATPase solubilized by the nonionic detergent octaethylene glycol monododecyl ether was studied by molecular sieve high-performance liquid chromatography (HPLC) and analytical ultracentrifugation [21].
• Molecular sieve HPLC shows that soluble sarcoplasmic reticulum Ca2+-ATPase at low concentrations of the non-ionic detergent octaethylene glycol monododecyl ether exists as monomers in equilibrium with dimers and higher oligomers [22].
• The oligomeric state of canine renal NA+/K+ -ATPase solubilized by octaethylene glycol n-dodecyl ether (C12E8) was studied by means of low-angle laser light scattering photometry coupled with high-performance gel chromatography (HPGC) [23].
• Molecular weights of three membrane proteins have been measured in the presence of 0.1% octaethylene glycol n-dodecyl ether (C12E8) by the measuring system in which a membrane protein eluted from a gel chromatography column is monitored sequentially for ultraviolet absorption, light scattering and refractive index [24].

References