The binding of sodium dodecyl sulphate to various proteins

Pitt‐Rivers, Rosalind; Impiombato, F. S. Ambesi

doi:10.1042/bj1090825

Cited by 493 publications

(168 citation statements)

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“…Moreover, if the degree of SDS adsorption by glycans found here (0.2 g/g) is general, the difference between peptides and glycans might be more pronounced for other glycoproteins. This suggestion is in accord with the study by Pitt-Rivers and Impiombato [21], who found that saturation occurred at around 1.0 g/g peptide for a range of different proteins whether glycosylated or not. While the contribution from the glycans cannot be unambiguously discerned from the variability among the different proteins studied by these workers, this result indeed suggests very low SDS binding to glycans.…”

Section: Discussionsupporting

confidence: 92%

“…To address the effects of glycosylation on the SDS-induced destabilization, and to determine the relative affinity of the detergent for the peptide and glycan moieties, we compared data for Phy with results for an enzymatically deglycosylated form (dgPhy). The importance of glycoprotein-surfactant interrelationships has been pointed out already in the seminal work of Pitt-Rivers and Impiomba [21], but none of the nearly 500 papers quoting this publication has addressed the problem. Recently, progress has been made in the understanding of surfactant interactions with soluble oligosaccharides [28][29][30][31], but protein conjugated glycans remain practically unexplored.…”

mentioning

confidence: 98%

“…This led to several general conclusions regarding the modes of interaction of SDS and proteins (for reviews see [18][19][20]). Thus, a certain pattern of binding events has been observed before the adsorption of surfactant eventually reached saturation at about 1.4 g SDS per g protein with reduced S-S bonds [15,21] and somewhat less (~1g/g) in proteins with intact cystines [21]. Some exceptions from this picture, however, have been reported.…”

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confidence: 99%

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Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Bagger

Hoffmann

Fuglsang

et al. 2007

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT2 AbstractThe interactions of sodium dodecyl sulfate (SDS) and two glyco-variants of the enzyme phytase from Peniophora lycii were investigated. One variant (Phy) was heavily glycosylated while the other (dgPhy) was enzymatically deglycosylated. Effects at 24°C of titrating SDS to Phy and dgPhy were studied by Isothermal Titration Calorimetry (ITC) and Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy. Comparisons of results for the two variants were used to elucidate glycan-surfactant interrelationships.The CD spectra suggested that both the native and the SDS-denatured states of the two variants were mutually similar, and hence that the denaturation process was structurally equivalent for the two glyco-variants.The denatured state was far from fully unfolded and probably retained a substantial content of native-like structure. Furthermore, it was found that the glycans brought about only a small increase in the resistance towards SDS induced denaturation. The SDS concentration required to denature half of the protein molecules differed less than 1 mM for the two variants.The affinity for SDS of both variants was unusually low. The amount of bound SDS (w/w) at different stages of the binding isotherm was 3-10 times lower than that reported for the most previously investigated globular proteins. Analysis of the relative affinity of the glycan and peptide moieties suggested that the carbohydrates bind much less surfactant. At saturation, glycans adsorbed about half as much SDS (in g/g) as the peptide moiety of Phy and about five times less than average proteins.

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Section: Discussionsupporting

confidence: 92%

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confidence: 98%

mentioning

confidence: 99%

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Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Bagger

Hoffmann

Fuglsang

et al. 2007

Biophysical Chemistry

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“…This is appreciably higher than the value of 0.9g/g found for the non-reduced protein by Pitt-Rivers & Impiombato (1968), presumably as a result of the higher concentration of sodium dodecyl sulphate used in the present work. The denaturation profiles, i.e.…”

Section: Resultscontrasting

confidence: 75%

Studies of the denaturation and partial renaturation of ovalbumin

Holt

Creeth

1972

Biochemical Journal

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1. The denaturation of ovalbumin by the reagents sodium dodecyl sulphate and guanidinium chloride was investigated, by following the changes in sedimentation velocity, optical rotatory dispersion and viscosity as a function of denaturant concentration. 2. With sodium dodecyl sulphate both the optical-rotatory-dispersion parameters ao and bo become more negative, the sedimentation coefficient decreases and the viscosity increases; significant differences in the denaturation profiles are observed. The change in each parameter is indicative of only limited denaturation. 3. With guanidinium chloride the transition occurs over the concentration range 1-4m: more extensive changes occur in all the physical parameters than with sodium dodecyl sulphate. The values of ao and bo are indicative of complete denaturation. Reduction by mercaptoethanol produces only minor further changes. 4. Renaturation was attempted from both denaturants, the removal of reagent being accomplished reversibly by controlled slow dialysis. Partial renaturation was observed, but aggregated or insoluble material was produced in both cases at relatively low concentrations of denaturant. Similar behaviour was observed with fully reduced protein in guanidinium chloride-mercaptoethanol; complete renaturation could not be brought about even at very low protein concentrations.

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“…Unreacted samples or crosslinked material were expected to migrate at different positions since it has been reported that, after reaction with dimethyl suberimidate, migration of proteins is slightly slowed down, probably because the binding of sodium dodecylsulfate is reduced after amidation [7]. Therefore two calibration curves have been established.…”

Section: Crorrlinking Bet Ween Subunits and Moleculur Weight De Fenmentioning

confidence: 99%

Physico‐chemical Properties of a DNA Binding Protein: Escherichia coli Factor H₁

Spassky

Buc

1977

European Journal of Biochemistry

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HI factor is a heat-stable protein found in large amounts in Escherichia coli. In vitro, this protein has been found to stimulate transcription of A templates by E. coli DNA-dependent RNA polymerase.The subunit molecular weight of this factor has been re-estimated and found to be 15500 IL-1000 in the presence of 2-mercaptoethanol. Crosslinking experiments performed with dimethylsuberimidate in the presence or absence of the DNA template indicate the presence of multiples of the 15 500-M, subunit up to the tetramer, the dimeric species being predominant. One cysteinyl residue per 15 000-M, subunit is labeled by 4-chloro-7-nitrobenzofurazan. This residue is not labeled if the factor is exposed to oxidizing conditions. In this case, three lysyl residues are titrated.HI factor behaves as a DNA-binding protein. We have detected binding to DNA by two independent methods : displacement of a fluorescently labeled factor by the native protein and retention of radioactive DNA on millipore filters in the presence of the factor. Under our experimental conditions (high ionic strength, abscnce of magnesium ions), the saturation function of A plac *DNA as well as of wild-type A DNA has been found to be non-cooperative. Saturation is reached when 300 k 30 molecules of dimeric factor are bound per R molecule, the average dissociation constant of the complex being 10 nM.The dissociation time of the HI -DNA complex is less than 5 s at 37 "C. The binding of this factor lowers the affinity of native DNA for ethidium bromide. In the presence of this intercalating dye, the solubility of the complex decreases drastically.In 1971, Jacquet et nl. described a heat-stable protein fraction from Esclzerichia coli which stimulated RNA synthesis directed by native , I or 480 DNA [l]. One year later, Cukier-Kahn el al. showed that this fraction could be resolved into several proteins. One of the stimulating factors, HI, was shown to be a low-molecular-weight protein having an isoelectric point close to 7. As the amount of HI required for maximal stimulation was proportional to the amount of DNA present in the assay in vitro, it was suggested that this factor stimulates DNA transcription by binding to the template and inducing a conformational change of the promotor [2]. It was later reported that promotors sensitive to catabolic repression were Abbreviutions. N bf-C1,4-chloro-7-nitroben70furazan (or 7-chloro-4-nitroben7o-2-oxa-1,3-diazole); fluorescamine, 4-phenylspiro-[furan-2(3),1 '-phthalan]-3,3-dione.Enzymes. RNA polymerase or nucleosidetriphosphatc : RNA nucleotidyltransferase (EC 2.7.7.6); beef pancreas deoxyribonuclease I (EC 3.1.4.5).better stimulated than others [3]. We have therefore undertaken a physico-chemical study of the interaction between this factor and two A DNA samples in order to investigate the structural basis of these observations. MATERIALS AND METHODS Prepration of D N A SamplesPhage DNAs, i plac imm 434 cS' S7 or A imm 434 cItS S7, were prepared as described elsewhere [4].Thermal induction of the lysogenic prophage wa...

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The binding of sodium dodecyl sulphate to various proteins

Cited by 493 publications

References 13 publications

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Studies of the denaturation and partial renaturation of ovalbumin

Physico‐chemical Properties of a DNA Binding Protein: Escherichia coli Factor H₁

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The binding of sodium dodecyl sulphate to various proteins

Cited by 493 publications

References 13 publications

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Glycoprotein-surfactant interactions: A calorimetric and spectroscopic investigation of the phytase-SDS system

Studies of the denaturation and partial renaturation of ovalbumin

Physico‐chemical Properties of a DNA Binding Protein: Escherichia coli Factor H1

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Product

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Physico‐chemical Properties of a DNA Binding Protein: Escherichia coli Factor H₁