Sodium Dodecyl Sulfate Analogs as a Potential Molecular Biology Reagent (original) (raw)
Related papers
Journal of Pure and Applied Microbiology
Dodonaea viscosa Jacq is known as “chamana” in the popular flora of Peru. The traditional medicine uses its leaves as ingredient in fermented beverages from Zea mays and also in external uses for anti-inflammatory diseases. The aim was to study the role of dodonic acid against several protein targets of S. aureus. This study was focused on to analyse the role of dodonic acid against S. aureus target proteins such as on Sortase-A, DNA gyrase, dihydrofolate reductase (DHFR), clumping factor, dehydrosqualene synthase, and undecaprenyl di-phosphate synthase as a promising candidate molecule. The docking analysis of dodonic acid showed the best docking score energy on S. aureus undecaprenyl diphosphate synthase with -11.2 kcal/mol and demonstrated to be a very stable molecule at physiological conditions during the molecular dynamic for 50 ns. As conclusion, the extract demonstrated to be active against S. aureus and dodonic acid might be a promising molecule acting on the S. aureus undec...
A micromethod for complete removal of dodecyl sulfate from proteins by ion-pair extraction
Analytical Biochemistry, 1979
Methods are presented for the complete removal of dodecyl sulfate from proteins. The methods utilize the extraction of dodecyl sulfate anions as ion pairs with triethylammonium or tributylammonium cations into an organic solvent. The protein is insoluble in the organic solvent and is recovered as a precipitate. The methods are applicable to microgram as well as milligram amounts of protein. In all cases studied, the recovery of protein ranges from 70 to 100%. The recovered protein is suitable for N-terminal Edman degradation, tryptic peptide mapping, and amino acid analysis and can be renatured to regain enzymatic activity and antigenicity.
Crystallisation of sodium dodecyl sulfate and the corresponding effect of 1-dodecanol addition
Journal of Crystal Growth, 2016
Link to publication on Research at Birmingham portal General rights Unless a licence is specified above, all rights (including copyright and moral rights) in this document are retained by the authors and/or the copyright holders. The express permission of the copyright holder must be obtained for any use of this material other than for purposes permitted by law. • Users may freely distribute the URL that is used to identify this publication. • Users may download and/or print one copy of the publication from the University of Birmingham research portal for the purpose of private study or non-commercial research. • User may use extracts from the document in line with the concept of 'fair dealing' under the Copyright, Designs and Patents Act 1988 (?) • Users may not further distribute the material nor use it for the purposes of commercial gain. Where a licence is displayed above, please note the terms and conditions of the licence govern your use of this document. When citing, please reference the published version. Take down policy While the University of Birmingham exercises care and attention in making items available there are rare occasions when an item has been uploaded in error or has been deemed to be commercially or otherwise sensitive.
Journal of applied microbiology, 2015
Biological synthesis of rhamnolipids from SDS by Pseudomonas aeruginosa S15 is found to be a cost effective mode of rhamnolipid synthesis. The current study aimed to attempt rhamnolipid synthesis by transformant Escherichia coli DH5α cells. Molecular analysis by curing experiments revealed that the properties of SDS based rhamnolipid synthesis were plasmid borne. Transformation of 10 kb plasmid to Escherichia coli DH5α cells conferred rhamnolipid synthetic ability to transformant. Various genetic elements involved in SDS based rhamnolipid synthesis were analyzed using PCR based and restriction digestion based approaches. PCR amplification using primers specific for sdsA gene encoding alkylsulfatases yielded two significant amplicons viz, 1.2 kb fragment and 422 bp fragment, coding for putative dehydratase and ABC transporter respectively. Amplicon of sdsB gene lacked ability of SDS degradation and rhamnolipid synthesis. Rhamnolipid biosynthesis by transformant E.coli DH5α containing...
Structure of dodecyl sulfate—protein complexes at subsaturating concentrations of free detergent
Biophysical Chemistry, 1994
Earlier neutron small-angle scattering experiments had revealed the low resolution structure of the complex between sodium dodecyl sulfate (SDS) and the single polypeptide (452 amino acid residues) of a water-soluble enzyme. The saturated complex consists of three globular micelles (c+-.) which are connected by short flexible polypeptide segments. New experiments, described here, were performed at subsaturating concentrations of free SDS in equilibrium with the complex. The data show a decrease in stoichiometry from one bound dodecyl sulfate (DS) anion per two amino acid residues near the critical micelle concentration (CMC) to one per four residues at half the CMC. At 0.3 CMC, a two-micelle complex (+-•) is formed by the recombination of the small amino-terminal micelle with the middle one; and the center-to-center distance between the carboxylterminal micelle and the middle one decreases from 7.5 to 6.2 nm. These structural data allow us to better understand earlier results obtained with high-performance agarose gel chromatography of the same SDS-protein complexes.
Applied and Environmental Microbiology, 2000
We identified trace metabolites produced during the anaerobic biodegradation of H 26-and D 26-n-dodecane by an enrichment culture that mineralizes these compounds in a sulfate-dependent fashion. The metabolites are dodecylsuccinic acids that, in the case of the perdeuterated substrate, retain all of the deuterium atoms. The deuterium retention and the gas chromatography-mass spectrometry fragmentation patterns of the derivatized metabolites suggest that they are formed by COH or COD addition across the double bond of fumarate. As trimethylsilyl esters, two nearly coeluting metabolites of equal abundance with nearly identical mass spectra were detected from each of H 26-and D 26-dodecane, but as methyl esters, only a single metabolite peak was detected for each parent substrate. An authentic standard of protonated n-dodecylsuccinic acid that was synthesized and derivatized by the two methods had the same fragmentation patterns as the metabolites of H 26-dodecane. However, the standard gave only a single peak for each ester type and gas chromatographic retention times different from those of the derivatized metabolites. This suggests that the succinyl moiety in the dodecylsuccinic acid metabolites is attached not at the terminal methyl group of the alkane but at a subterminal position. The detection of two equally abundant trimethylsilyl-esterified metabolites in culture extracts suggests that the analysis is resolving diastereomers which have the succinyl moiety located at the same subterminal carbon in two different absolute configurations. Alternatively, there may be more than one methylene group in the alkane that undergoes the proposed fumarate addition reaction, giving at least two structural isomers in equal amounts.
Analytical Biochemistry, 1985
A procedure is described for the determination of the Stokes radius of a detergent micelie by gel chromatography. It was observed that different lots of Sepharose -4B can exhibit a wide variation in the permeation of their gel pores. It is shown that this variation is due to differences in their pore size distribution. It has been observed that protein-sodium dodecyl sulfate (SDS) complexes of high Stokes radii eluted on a Sepharose 4B column with Stokes radii lower than the theoretical, as it has been previously reported but that protein-SDS complexes of low Stokes radii (~70 A), contrary to what might have been expected. eluted with Stokes radii higher than the theoretical. Evidence was obtained that their anomalous elution is due to an interaction of the detergent SDS with the gel pores of small diameter. cn 198j Academic PRESS. IX