Study of solubility of indicator dyes in aqueous solution of pure and binary mixed surfactants. Aggregation and microenvironmental properties of homo and hetero-micelles of triton X 100 and sodium dodecyl sulphate

2008 ◽  
Vol 139 (1-3) ◽  
pp. 104-109 ◽  
Author(s):  
Angshuman Maitra ◽  
Nipamanjari Deb ◽  
Sanjib Bagchi
Keyword(s):  
Aqueous Solution ◽  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Mixed Surfactants ◽  
Binary Mixed Surfactants ◽  
Indicator Dyes ◽  
Triton X

Solubilization and immunoprecipitation of 125I-labelled antigens from Plasmodium knowlesi schizont-infected erythrocytes using non-ionic, anionic and zwitterionic detergents

Parasitology ◽  
1984 ◽  
Vol 88 (1) ◽  
pp. 27-36 ◽  
Author(s):  
R. J. Howard ◽  
J. W. Barnwell
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Plasmodium Knowlesi ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Ionic Detergents ◽  
Class A ◽  
Anionic Detergents ◽  
Triton X

SUMMARYPlasmodium knowlesi malaria-infected erythrocytes were radio-iodinated and several non-ionic, anionic and zwitterionic detergents were compared in their capacity to extract the labelled membrane proteins. The use of these detergents for antigen identification was tested by immunoprecipitation, after addition of Triton X-100 to some detergent extracts, using hyperimmune monkey antiserum and protein A-Sepharose. 125I-labelled antigens were specifically immunoprecipitated with all detergents tested, including the anionic detergents sodium dodecyl sulphate (SDS), deoxycholate and cholate; the zwitterions Zwittergent-312 and -314, CHAPS and Empigen BB, as well as several non-ionic detergents. The SDS-polyacrylamide gel electrophoresis patterns of 125I-labelled antigens varied after extraction with different detergents, there being no consistent pattern for detergents of a particular class. A total of 14 125I-labelled antigens were identified, 11 of them using Triton X-100. Some minor antigens identified with Triton X-100 were immunoprecipitated in greater amount after extraction in other detergents. Most importantly, two antigens Mr 200000 and 180000 were detected only after extraction with deoxycholate or SDS.

The outer membrane of Haemophilus influenzae type b: cell envelope associations of major proteins

1983 ◽  
Vol 29 (2) ◽  
pp. 280-287 ◽  
Author(s):  
J. W. Coulton ◽  
D. T. F. Wan
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Cell Envelope ◽  
Sodium Dodecyl ◽  
Haemophilus Influenzae Type ◽  
Major Protein ◽  
Haemophilus Influenzae Type B ◽  
Type B ◽  
Molecular Weights ◽  
Triton X

Membrane proteins fom the cell envelope of Haemophilus influenzae type b ATCC 9795 were examined by sodium dodecyl sulphate – polyacrylamide gel electrophoresis. When envelopes were extracted with a phosphate-based buffer containing 2% Triton X-100, a major protein of molecular weight 43 000 was detected in fractions containing cytoplasmic membrane proteins. The cell wall material which was Triton X-100 insoluble contained six major proteins of molecular weights 46 000, 40 000, 36 000, 30 000, 27 000, and 16 000. One of these proteins showed a shift in molecular weight from 27 000 to 36 000 when it was heated over a temperature range from 50 °C to 100 °C in buffer containing 2% sodium dodecyl sulphate, 5% 2-mercaptoethanol. This alteration in mobility could be demonstrated either by the membrane-bound form of the protein or by a detergent-soluble form of the protein. Enriched preparations of the 36 000 molecular weight form were obtained by a series of purification steps. Extraction of the Triton X-100 insoluble material with buffer containing 2% Triton X-100, 5.0 mM EDTA yielded chiefly one major protein molecular weight 30 000 and many minor protein species. Pretreatment of the Triton X-100 insoluble fraction with lysozyme followed by extraction with buffer containing 2% Triton X-100, 5.0 mM EDTA released two proteins of molecular weights 16 000 and 27 000 and few minor proteins. By these operational manipulations, the proteins of molecular weights 16 000 and 27 000 may be considered as peptidoglycan-associated proteins.

Metal-free synthesis of polysubstituted pyrroles using surfactants in aqueous medium

2017 ◽  
Vol 19 (22) ◽  
pp. 5385-5389 ◽  
Author(s):  
Amrendra Kumar ◽  
Ramanand Ramanand ◽  
Narender Tadigoppula
Keyword(s):  
Aqueous Medium ◽  
Sodium Dodecyl Sulphate ◽  
Room Temperature ◽  
Sodium Dodecyl ◽  
Pyrrole Derivatives ◽  
Metal Free ◽  
Triton X

An efficient and metal-free method has been developed for the synthesis of polysubstituted pyrrole derivatives with combination of sodium dodecyl sulphate (SDS) and Triton X-100 surfactants using water as a solvent at room temperature in 2–6 h and under microwave conditions (10 min) with good to excellent yields.

scholarly journals Protein chromatography on adsorbents with hydrophobic and ionic groups. Purification of human erythrocyte glycophorin

1977 ◽  
Vol 163 (2) ◽  
pp. 397-400 ◽  
Author(s):  
R J Simmonds ◽  
R J Yon
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Human Erythrocyte ◽  
Sodium Dodecyl ◽  
Erythrocyte Ghosts ◽  
Electrophoretic Band ◽  
Protein Chromatography ◽  
Ionic Groups ◽  
A Subunit ◽  
Triton X

Human erythrocyte glycophorin was purified rapidly by (a) chromatography of a Triton X-100 extract of erythrocyte ‘ghosts’ on N-(3-carboxypropionyl)aminodecyl-Sepharose in buffers containing Triton X-100 or sodium dodecyl sulphate, or (b) chromatography of whole ‘ghosts’, solubilized in sodium dodecyl sulphate, on dodecyl-Sepharose, in buffers containing sodium dodecyl sulphate. The products contained 85-95% glycophorin (electrophoretic band PAS-1) and the major contaminants were glycoproteins PAS-2 (possibly a subunit of glycophorin) and PAS-3.

Conductometric and fluorometric studies of sodium dodecyl sulphate in aqueous solution and in the presence of amino acids

2014 ◽  
Vol 112 (20) ◽  
pp. 2681-2693 ◽  
Author(s):  
Anwar Ali ◽  
Nisar Ahmad Malik ◽  
Sahar Uzair ◽  
Maroof Ali
Keyword(s):  
Aqueous Solution ◽  
Amino Acids ◽  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl

High-speed gel filtration of proteins in sodium dodecyl sulphate aqueous solution on TSK-GEL SW type

1980 ◽  
Vol 193 (1) ◽  
pp. 29-36 ◽  
Author(s):  
Yoshio Kato ◽  
Katsuo Komiya ◽  
Hiroo Sasaki ◽  
Tsutomu Hashimoto
Keyword(s):  
Aqueous Solution ◽  
Sodium Dodecyl Sulphate ◽  
High Speed ◽  
Sodium Dodecyl ◽  
Gel Filtration

scholarly journals The molecular size of N-methylglutamate dehydrogenase of Pseudomonas aminovorans

1977 ◽  
Vol 167 (2) ◽  
pp. 509-512 ◽  
Author(s):  
C W Bamforth ◽  
P J Large
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Molecular Size ◽  
Partial Specific Volume ◽  
Triton X

N-Methylglutamate dehydrogenase, purified to a specific activity of 0.29 unit/mg of protein, gave one band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, corresponding to a molecular weight of 130 000. Enzyme-Triton complexes were found to have a partial specific volume of 0.73 cm3/g, suggesting that the protein binds less than 0.1 g of Triton/g of protein. A molecular weight for the intact enzyme in the presence of 1% (w/v) Triton X-100 of 550 000 suggested that the enzyme may be a tetramer.

scholarly journals Affinity chromatography of human plasma low- and high-density lipoproteins. Elution by selective cleavage of a bond in the spacer

1979 ◽  
Vol 181 (3) ◽  
pp. 691-698 ◽  
Author(s):  
A Wichman
Keyword(s):  
Human Plasma ◽  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
High Capacity ◽  
High Density ◽  
High Density Lipoproteins ◽  
Protein Solutions ◽  
Ester Bond ◽  
Triton X

Human plasma low- and high-density lipoproteins were found to bind to Sepharose gels containing coupled cholesterol or cholic acid. The lipoproteins were bound very strongly, and it was not possible to elute them under non-denaturing conditions. The detergents Triton X-100 and sodium dodecyl sulphate eluted the lipoproteins in partly denatured form. Adsorbents were used where the steroid was coupled through a spacer containing a thiol ester bond. It was thus possible to elute bound lipoproteins by selective cleavage of the bond with hydroxylamine. A small proportion of albumin was the only contaminant detected, the amounts depending on which ligand was used. Low- and high-density lipoproteins were separated by gel filtration. They behaved as did the native molecules when analysed by gel filtration, immunodiffusion, immunoelectrophoresis and electrophoresis in polyacrylamide gradient gels. The high capacity and the selectivity of the adsorbents make them suitable for the removal of lipoproteins from protein solutions.

The action of Triton X-100 and sodium dodecyl sulphate on lipid layers. Effect on monolayers and liposomes

1990 ◽  
Vol 7 (2) ◽  
pp. 255-259 ◽  
Author(s):  
Jordi Hernández Borrell ◽  
Miquel Pons ◽  
Juan C. Juarez ◽  
Joan Estelrich
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Triton X ◽  
Lipid Layers
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