Disease relevance of dimethyl-myristyl-(3-sulfopropyl)ammonium

• The proton-translocating F1F0 ATP synthase from Clostridium thermoautotrophicum was solubilized from cholate-washed membranes with Zwittergent 3-14 at 58 degrees C and purified in the presence of octylglucoside by sucrose gradient centrifugation and ion-exchange chromatography on a DEAE-5PW column [1].
• In order to assess the systemic toxicity of Zwittergent 3-14, a detergent used in the protein-detergent complex vaccines for its attractive immunogenic properties, a subacute toxicity study was performed [2].
• A major cell envelope protein was purified from the cell envelope fraction of Treponema denticola ATCC 35405 by ion exchange chromatography after extraction with Zwittergent 3-14 [3].

High impact information on dimethyl-myristyl-(3-sulfopropyl)ammonium

• Protein P2 from these prototype isolates was solubilized with Zwittergent 3-14 and purified to homogeneity [4].
• We solubilized cardiolipin synthase from rat liver mitochondrial membranes with Zwittergent 3-14 and purified it by Mono Q anion exchange chromatography, Superose 12 gel filtration, and Mono P chromatofocusing [5].
• The subunit structure of the rabbit skeletal muscle ryanodine receptor-Ca2+ release channel complex was examined following solubilization of heavy sarcoplasmic reticulum membranes in two zwitterionic detergents, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (Chaps) and Zwittergent 3-14 [6].
• Incubation of P. intermedia cells in the presence of Zwittergent 3-14 allowed complete solubilization of the Fc receptor from the cell surface [7].
• In order to characterize these mucin-binding adhesins, outer membrane proteins (OMP) from two adhesive strains, 1244-NP and PAK-NP, and their poorly adhesive rpoN mutants, 1244-N3 and PAK-N1, were prepared by a mild extraction with Zwittergent 3-14 [8].

Biological context of dimethyl-myristyl-(3-sulfopropyl)ammonium

• For example, a BGE comprising 10 mM Zwittergent-3-14, 50 mM Tween 20, 0.3 M NaCl and 5 mM phosphate (ph 7) could be used for the determination of UV-absorbing anions in seawater, giving good peak shapes and detection limits of 0.8 microM and 0.6 microM for nitrate and bromide, respectively [9].

Anatomical context of dimethyl-myristyl-(3-sulfopropyl)ammonium

• Triton X-100, and Zwittergent 3-14, had its own advantages and drawbacks as myelin protein extractors [10].
• After cell lysis and harvesting by centrifugation, the inclusion bodies were solubilized in Zwittergent 3-14 solution and refolded by stepwise dilution [11].
• [D]50 values were determined for caput (immature) and cauda (mature) ram epididymal spermatozoa with four detergents (cetyltrimethylammonium bromide, sodium dodecylsulfate, Zwittergent 3-14, and sodium deoxycholate) [12].
• TPO was purified from human thyroid tissue by: (1) isolation of thyroid microsomes using homogenization and differential centrifugation, (2) solubilization of membrane proteins by Zwittergent 3-14, and (3) anion exchange liquid chromatography on a FPLC Mono Q column [13].
• Oxidation-reduction (O-R) ratios of extracts varied with detergent used and ranged from 0.18 (CHAPS) to 3.8 (Zwittergent 3-14) relative to a ratio of 1.7 in intact microsomes [14].

Associations of dimethyl-myristyl-(3-sulfopropyl)ammonium with other chemical compounds

• Extraction conditions for P400 protein were investigated, and complete solubilization of P400 protein from a submicrosomal fraction (P31 fraction) of mouse cerebellum was attained by the combination of 4% Zwittergent 3-14 and 4 M guanidinium chloride [15].
• Using a reversed-phase C18 column (250x4.6 mm I.D.) coated with 10/10 (mM/mM) of TTA/Zwittergent-3-14 mixed micelles as the stationary phase and either NaHCO3 or Na2CO3 aqueous solution as the eluent, together with suppressed conductivity detection, baseline separation of seven model inorganic anions was obtained [16].

Gene context of dimethyl-myristyl-(3-sulfopropyl)ammonium

• The purified and denatured protein BacP1 was solubilized in SDS, followed by addition of an excess of a second detergent (Zwittergent 3-14 or Triton X-100) [17].
• 1. Mitochondrial rat kidney transamidinase was solubilized by two extractions with the surfactant Zwittergent 3-14 [18].
• Cardiolipin synthase has been purified to near-homogeneity from rat liver by solubilization with Zwittergent 3-14 followed by FPLC anion exchange, gel permeation and chromatofocusing steps [19].

Analytical, diagnostic and therapeutic context of dimethyl-myristyl-(3-sulfopropyl)ammonium

• The purified complex migrated as a single peak with an apparent sedimentation coefficient of approximately 30 and approximately 9 S upon density gradient centrifugation and with isoelectric points of 3.7 and 3.9 upon two-dimensional gel electrophoresis in Chaps and Zwittergent 3-14, respectively [6].
• The method involves solubilization of the MOMP with Zwittergent 3-14 and further purification accomplished by ion-exchange and molecular-sieve chromatographies [20].
• Western blot analyses revealed several outer membrane proteins in the zwittergent 3-14 extract [21].
• As seen on SDS/PAGE, the 38 kDa band completely migrated to approximately 110 kDa when the purified monomeric proteins were refolded in a buffer system containing 10% (w/v) Zwittergent 3-14, together with a subsequent heating to 95 degrees C for 5 min [22].

References