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PubMed2005

The role of detergent in refolding of GdnHCl-denatured arginine kinase from shrimp Fenneropenaeus Chinensis: the solubilization of aggregate and refolding in detergent solutions.

Strong aggregation occurred in the refolding route of arginine kinase (AK) denatured with 3 mol GdnHCl/L (GdnHCl, guanidine hydrochloride). The activity recovery of GdnHCl-denatured AK was very low and dependent on the protein concentration in the process of refolding. For denatured AK at 1.2 micromol/L concentration, the recovered activity yield was about 45.2% of the native enzyme, whereas at 5.2 micromol/L the activity recovery yield was only 20% of native activity. The nonionic detergent Triton X-100 and Tween 20 (< or = 100 mmol/L concentration) not only effectively blocked the aggregation but also enabled the denatured AK to recover most of its native activity. The kinetics of aggregate solubilization showed that there was an induction phase dependent on the detergent, but there was no dependency when detergent was absent. The apparent activity recovery had a cooperative relation with detergents in the process of refolding, which suggested the existence of some interaction between the detergent and the refolding intermediate. On the basis of the study results, a scheme of refolding was proposed.

Animals↗

PubMed1997

Correlation of acid detergent lignin and Klason lignin with digestibility of forage dry matter and neutral detergent fiber.

The acid detergent lignin and Klason lignin methods were compared for their correlation with forage digestibility. Thirty-six forages, including C3 legumes and C3 and C4 grasses, were analyzed for sulfuric acid detergent lignin, Klason lignin, and in vitro digestibilities of dry matter (DM) and neutral detergent fiber (NDF). Twenty of these forages were also fed to lambs at restricted intake for measurement of DM and NDF digestibilities. Lignin concentrations determined by the two lignin methods were positively correlated, and the Klason lignin value was always greater than the acid detergent lignin concentration. The largest differences were observed for grass forages. Digestibilities of forage DM and NDF were negatively correlated with both lignin methods for the in vitro system and the lamb digestibility trials. The degree of correlation for the two lignin methods with digestibility was generally similar across all forages and within forage classes. Slopes of linear regressions of digestibility on lignin concentration did not differ between legumes and grasses. Although the sulfuric acid detergent lignin and Klason lignin procedures gave very different estimates of forage lignin concentration, they were similarly correlated with digestibility and should yield predictions of forage digestibility that have similar accuracy.

Animal Feed↗

PubMed1986

Metal-ion assisted detergent action on bacterial growth: detergent specificity and mechanism of inhibition.

Detergents in general inhibit bacterial growth. The anionic detergent, sodium lauryl sulphate (NaLS), seems to have a more specific inhibitory effect on growth of the Gram-positive Bacillus subtilis than on growth of the Gram-negative Escherichia coli. The specificity of anionic detergent towards B. subtilis has been traced to the difference in the nature of the cell wall. The inhibitory action of the detergent is markedly increased by the presence of metal ions like Cd++ or Mg++, due probably to the increase in the micellar phase, facilitating the solubilisation of bacterial species in the inner core of micelles. While metal ions like Cu++ do not influence the activity of NaLS, Na+, Ca++ or Mn++ ions seem to act against the detergent action on bacterial growth, probably by altering the structure of micelles.

Bacillus subtilis↗

PubMed1996

Monomeric human red cell glucose transporter (Glut1) in non-ionic detergent solution and a semi-elliptical torus model for detergent binding to membrane proteins.

The self-association state of the human red cell glucose transporter (Glut1) in octaethylene glycol n-dodecyl ether (C12E8) and n-octyl beta-D-glucopyranoside (OG) solution was analyzed in the presence of reductant by gel filtration with light-scattering, refractivity and absorbance detection, and by ultracentrifugation. The C12E8-Glut1 complex was essentially monomeric, whereas OG-Glut1 also formed dimers and larger oligomers. C12E8-Glut1 retained substantial glucose transport activity even after depletion of endogenous lipids by gel filtration, as shown by reconstitution and transport measurements. Removal of endogenous lipids from OG-Glut1 abolished the activity unless phosphatidylcholine was included in the eluent. The binding of C12E8 and OG to Glut1 was determined by gel filtration with refractivity and absorbance detection or with radioactive tracer to be 1.86 +/- 0.07 and 1.84 +/- 0.09 g/g polypeptide, respectively. A structural model was proposed in which non-ionic detergent forms a semi-elliptical torus (SET) surrounding the transmembrane protein. The torus thickness was assumed to be equal to the radius (short half-axis) of a spherical (oblate ellipsoidal) free detergent micelle and the polar head groups of the detergent molecules were predicted to be situated just outside the hydrophobic surface of the protein. The experimental detergent binding values and those obtained from the SET model together confirmed that Glut1 was monomeric in C12E8 solution and provided constraints on the shape and size of the hydrophobic transmembrane region of Glut1 in alpha-helical and beta-barrel topology models.

Biological Transport↗

PubMed1985

An in vitro cytotoxicity test to predict the ocular irritation potential of detergents and detergent products.

Two in vitro cytotoxicity procedures, the measurement of cell-membrane integrity using fluorescein diacetate and ethidium bromide, and the quantitation of the release of a cell-membrane-bound enzyme, alkaline phosphatase, were used to assess the cytotoxicity of a range of cationic, anionic and nonionic detergents. The in vitro results were compared with the in vivo irritancy of these compounds in the rabbit eye. Although in general the decreasing order of potency of cationic, anionic and nonionic detergents was similar in vivo and in vitro, there were some apparent anomalies which may be due to the differing penetration characteristics of the detergents, as indicated by electrical impedance measurements of the isolated cornea. The study was extended to an examination of the cytotoxicity of a range of completely soluble, detergent-based formulations in a suspension culture of mouse fibroblasts. In this case the in vitro results correlated more closely with those from the in vivo tests.

Alkaline Phosphatase↗

PubMed2002

Detergent-free domain isolated from Xenopus egg plasma membrane with properties similar to those of detergent-resistant membranes.

Microdomains known as "rafts" have been isolated from many cell types as detergent-resistant membranes (DRMs) and are enriched in sphingolipids and cholesterol. However, there has been considerable controversy over whether such domains are found in native membranes or are artificially generated by the purification procedure. This controversy is based at least in part on the fact that raft membranes were first detected following detergent extraction in the cold. We isolated two plasma membrane fractions, without detergent treatment, using a discontinuous sucrose density gradient. One fraction was designated "light" and the other "heavy." These fractions were compared with DRMs, which were isolated in the presence of 1% Triton X-100. We found that Xenopus DRMs are enriched with sphingomyelin and cholesterol and exhibit a phase state similar to the liquid-ordered phase. Comparison of DRM complexes with the light and heavy plasma membrane fractions revealed some physical and biochemical similarities between the light fraction of the plasma membrane and the DRM complexes, based on (1) the phosphatidylcholine/sphingomyelin ratio and (2) the protein composition visualized on a two-dimensional gel. These two fractions are also quite similar in their thermotropic phase behavior, and their high levels of ganglioside GM1. We conclude that the light membrane fraction isolated in a detergent-free environment has many of the characteristics normally associated with DRMs.

Animals↗

PubMed2005

Dominant portion of thyrotropin-releasing hormone receptor is excluded from lipid domains. Detergent-resistant and detergent-sensitive pools of TRH receptor and Gqalpha/G11alpha protein.

Some G protein-coupled receptors might be spacially targetted to discrete domains within the plasma membrane. Here we assessed the localization in membrane domains of the epitope-tagged, fluorescent version of thyrotropin-releasing hormone receptor (VSV-TRH-R-GFP) expressed in HEK293 cells. Our comparison of three different methods of cell fractionation (detergent extraction, alkaline treatment/sonication and mechanical homogenization) indicated that the dominant portion of plasma membrane pool of the receptor was totally solubilized by Triton X-100 and its distribution was similar to that of transmembrane plasma membrane proteins (glycosylated and non-glycosylated forms of CD147, MHCI, CD29, CD44, transmembrane form of CD58, Tapa1 and Na,K-ATPase). As expected, caveolin and GPI-bound proteins CD55, CD59 and GPI-bound form of CD58 were preferentially localized in detergent-resistant membrane domains (DRMs). Trimeric G proteins G(q)alpha/G(11)alpha, G(i)alpha1/G(i)alpha2, G(s)alphaL/G(s)alphaS and Gbeta were distributed almost equally between detergent-resistant and detergent-solubilized pools. In contrast, VSV-TRH-R-GFP, Galpha, Gbeta and caveolin were localized massively only in low-density membrane fragments of plasma membranes, which were generated by alkaline treatment/sonication or by mechanical homogenization of cells. These data indicate that VSV-TRH-R-GFP as well as other transmembrane markers of plasma membranes are excluded from TX-100-resistant, caveolin-enriched membrane domains. Trimeric G protein G(q)alpha/G(11)alpha occurs in both DRMs and in the bulk of plasma membranes, which is totally solubilized by TX-100.

Caveolin 1↗

PubMed1998

Effect of non-ionic detergents on apparent enzyme mechanism: V121A mutant of Streptomyces cholesterol oxidase endowed with enhanced sensitivity towards detergents.

One of the mutants of Streptomyces cholesterol oxidase with the Val121Ala mutation (V121A) was kinetically analysed. Although the reaction rate-substrate concentration curve of wild type follows a simple Michaelis-Menten equation, that of V121A is sigmoidal. The cooperativity was apparent and caused by non-ionic detergents that were used as a solvent of cholesterol. The concentration dependence of V121A on detergents was more significant than that of wild type, although the reaction rates of both enzymes decrease as the concentrations of detergents increase. Further experiments suggested that less hydrophobic interactions between V121A and detergents should be responsible for the apparent cooperativity. Since Val121 is in a hydrophobic loop located near the active site, the mutational effect is structurally discussed.

Binding Sites↗

PubMedDate not supplied

The influence of detergent, the active component of detergent and sodiumtripolyphosphate on the biochemical process of some fungi.

Detergent "Merix" (Merima-Krusevac) and its components, sodiumtripolyphosphate and ethoxyled oleyl-cetyl alcohol in defined concentrations have influence on the enzymatic activity, bioproduction of amino acids and proteins and total biomass of species Aspergillus niger (A. niger) and Fusarium oxysporum (F. oxysporum). Detergent in concentration of 1% vol., in some cases, significantly stimulated production of the majority of amino acids. Detergent and its components (ethoxyled oleyl-cetyl alcohol and sodiumtripolyphosphate) in concentration of 1% vol. showed different influences on the production of proteins by the species of fungi A. niger and F. oxysporum. The enzymatic activity of fungi A. niger and F. oxysporum changed from total inhibition up to partial or total stimulation under influence of investigated pollutants. Detergent, sodiumtripolyphosphate and ethoxyled oleyl-cetyl alcohol, all in concentration of 1% vol. have reduced the production of the biomass of fungi A. niger and F. oxysporum. Investigated fungi have shown different response to the used pollutants.

Aspergillus niger↗

PubMedDate not supplied

The influence of detergents and active components of detergent on bioproduction of organic matters and enzymatic activity of some species of fungi.

Detergent (Merix, "Merima " Krusevac) applied in concentration of 1% vol. showed specific influence on the bioproduction of some 15 different amino acids and on the enzyme activity of the species of fungi A. niger, A. alternata and T. roseum. Detergent has significantly stimulated the production of 15 analyzed amino acids of the fungi species A. niger. The same applied concentration of detergent has decreased or considerably decreased the production of some 14 of totally 15 analyzed amino acids of investigated fungi species A. alternata and T. roseum. The enzyme activity of the fungi A. niger was more intensive in relation to the species A. alternata and T. roseum during the experimental period or in some phases of the experimental period. The detergent component, ethoxyled oleyl-cetyl alcohol, in concentration of 0.01%, 0.1% and 1% showed an inhibitory effect, or significant inhibitory effect on the enzyme activity of the examined species of fungi (A. niger, A. alternata and T. roseum).

Alternaria↗

PubMed1978

Interaction of lipopolysaccharide with detergents and its possible role in the detergent resistance of the outer membrane of Gram-negative bacteria.

In the presence of MgCl2, amounts of detergents which disrupted phospholipid vesicles caused lipopolysaccharide I from Proteus mirabilis to aggregate and form vesicular, membrane-like structures. Vesicle formation with P. mirabilis lipopolysaccharide II containing longer O-polysaccharide chains was extremely poor. Lipopolysaccharides of Salmonella minnesota R mutants (chemotypes Ra, Rc and Re) displayed a growing tendency for vesicle formation with increasing deficiency of the R core polysaccharide. Lipopolysaccharides of chemotypes Rc and Re produced vesicles even in the absence of MgCl2 and detergent. Spherical aggregates consisting of P. mirabilis lipopolysaccharide I MgCl2 and detergent were unable to either entrap or retain [14C]-sucrose, [3H=inulin or [3H]dextran. On the other hand, S. minnesota R mutant lipopolysaccharides of chemotypes Rc and Re could entrap all three saccharides and retain them for at least short periods of time. Leakage of [3H]-inulin out of re-lipopolysaccharide vesicles was greatly retarded by addition of MgCl2 to the vesicle system. Incorporation of P. mirabilis lipopolysaccharide I or S. minnesota Rc lipopolysaccharide into phospholipid vesicles protected these model membranes from disruption by detergent. This suggested a similar protective function of lipopolysaccharide in the outer membrane of enteric bacteria against the action of surfactants occurring in their normal intestinal habitat.

Biological Transport↗

PubMed1990

Surgical hand disinfection: comparison of 4% chlorhexidine detergent solution and 2% triclosan detergent solution.

The effect of 4% chlorhexidine detergent and 2% triclosan detergent on the resident flora of the hands was compared on 20 healthy volunteers. The initial and prolonged effects of the agents were assessed by a modification of the Peterson glove rinse test after multiple hand washes. Chlorhexidine detergent was significantly more effective than triclosan detergent (p less than 0.001) which in turn was more effective than non-medicated soap (p less than 0.001) for both initial and prolonged effect. Chlorhexidine, but not triclosan, showed a significantly greater prolonged effect than initial effect (p less than 0.01). Five volunteers (25%) experienced skin irritation with triclosan; no side effects were experienced with chlorhexidine.

Chlorhexidine↗

PubMed1988

A comparison of the effects of preoperative whole-body bathing with detergent alone and with detergent containing chlorhexidine gluconate on the frequency of wound infections after clean surgery. The European Working Party on Control of Hospital Infections.

In a prospective, randomized, double-blind, placebo-controlled study involving 27 surgical units in six European countries, the effect of preoperative whole-body bathing on two occasions with a detergent containing chlorhexidine (CHX+) on the incidence of wound infection in elective, clean surgery was compared with two bathings with a detergent without chlorhexidine (CHX-). In the CHX+ group 2.62% of 1413 patients and in the CHX- group 2.36% of 1400 patients subsequently became infected. The infection rate in the CHX+ group was 1.11 times that in the CHX- group with 95% confidence limits ranging between 0.69 and 1.82. Consequently, bathing patients twice preoperatively with chlorhexidine-detergent did not reduce the incidence of infection of clean wounds.

Adolescent↗

PubMed2005

Enzymatic detergent formulation containing amylase from Aspergillus niger: a comparative study with commercial detergent formulations.

There is a wide range of biotechnological applications for amylases, including the textile, pharmaceutical, food and laundry industries. Hydrolytic enzymes are 100% biodegradable and enzymatic detergents can achieve effective cleaning with lukewarm water. Microorganisms and culture media were tested for amylase production and the best producer was Aspergillus niger L119 (3.9 U ml(-1) +/- 0.2) in submerged culture and its amylase demonstrated excellent activity at 50-55 degrees C and pH 4.0, remaining stable at 53 degrees C for up to 200 h. In order to establish the potential uses of this enzyme in detergents, different formulations were tested using the A. niger amylase extract. Enzyme activity was compared with three commercial formulations. The detergents are used in hospitals to clean surgical and endoscopy equipment. The presence of amylase in the formulation is because of its action within hospital drainage system, whether or not it has any function in cleaning the equipment.

Amylases↗

PubMed2002

Structure, composition, and peptide binding properties of detergent soluble bilayers and detergent resistant rafts.

Lipid bilayers composed of unsaturated phosphatidylcholine (PC), sphingomyelin (SM), and cholesterol are thought to contain microdomains that have similar detergent insolubility characteristics as rafts isolated from cell plasma membranes. We chemically characterized the fractions corresponding to detergent soluble membranes (DSMs) and detergent resistant membranes (DRMs) from 1:1:1 PC:SM:cholesterol, compared the binding properties of selected peptides to bilayers with the compositions of DSMs and DRMs, used differential scanning calorimetry to identify phase transitions, and determined the structure of DRMs with x-ray diffraction. Compared with the equimolar starting material, DRMs were enriched in both SM and cholesterol. Both transmembrane and interfacial peptides bound to a greater extent to DSM bilayers than to DRM bilayers, likely because of differences in the mechanical properties of the two bilayers. Thermograms from 1:1:1 PC:SM:cholesterol from 3 to 70 degrees C showed no evidence for a liquid-ordered to liquid-disordered phase transition. Over a wide range of osmotic stresses, each x-ray pattern from equimolar PC:SM:cholesterol or DRMs contained a broad wide-angle band at 4.5 A, indicating that the bilayers were in a liquid-crystalline phase, and several sharp low-angle reflections that indexed as orders of a single lamellar repeat period. Electron density profiles showed that the total bilayer thickness was 57 A for DRMs, which was approximately 5 A greater than that of 1:1:1 PC:SM:cholesterol and 10 A greater than the thickness of bilayers with the composition of DSMs. These x-ray data provide accurate values for the widths of raft and nonraft bilayers that should be important in understanding mechanisms of protein sorting by rafts.

1,2-Dipalmitoylphosphatidylcholine↗

PubMed2003

Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts.

Specific proteins and lipids sequester to regions of cell membranes called rafts. Due to their high content of sphingomyelin (SM) and cholesterol, raft bilayers are thicker than nonraft bilayers and, at least at 4 degrees C, are resistant to Triton X-100 extraction. It has been postulated that rafts concentrate proteins with long transbilayer domains because of "hydrophobic matching" between the transbilayer domain and the thick bilayer hydrocarbon region. However, because the area compressibility and bending moduli of SM:cholesterol bilayers are larger than that of nonraft bilayers, there should be an energy cost to partition proteins or peptides into rafts. To determine the effects on peptide sorting of raft thickness and mechanical properties, we incorporated two transbilayer peptides (P-23, P-29) into bilayers composed of SM, dioleoylphosphatidylcholine, and cholesterol, separated detergent-soluble membranes (DSMs) from detergent-resistant membranes (DRMs), and measured their peptide and lipid compositions. P-23 and P-29 were designed to have transbilayer domains that matched the hydrocarbon thicknesses of DSMs and DRMs, respectively. At both 4 degrees C and 37 degrees C DSMs were enriched in dioleoylphosphatidylcholine and DRMs were enriched in SM and cholesterol. At both temperatures both P-23 and P-29 preferentially localized to DSMs, demonstrating the importance of bilayer mechanical properties relative to hydrophobic mismatch. However, at 37 degrees C significantly more P-29 than P-23 was located in DRMs, implying that hydrophobic matching played a role in peptide sorting at physiological temperature. These experiments demonstrate that the sorting of peptides as measured by detergent extraction is temperature-dependent and both bilayer mechanical properties and hydrophobic matching impact peptide distribution between DSMs and DRMs.

Animals↗

PubMed1999

Ion-exchange chromatography separation of the detergent and the solvent from immunoglobulins after solvent-detergent treatment.

For inactivation of lipid-enveloped viruses during the immunoglobulin production, the solvent-detergent (S/D) method was applied. Tri-n-butyl phosphate (solvent) and Triton X-100 (detergent) were removed from S/D treated immunoglobulins by ion-exchange chromatography on Q-Sepharose Fast Flow (FF). During the chromatographic procedure immunoglobulins remained bound on a Q-Sepharose FF, whereas solvent and detergent were eluted by washing with starting buffer. Elution of immunoglobulins was achieved by increasing the ionic strength of the starting buffer. The final immunoglobulin preparation contained less than 10 microg/ml of Triton X-100 and less than 2 microg/ml tri-n-butyl phosphate. It was confirmed that the S/D procedure did not cause a significant change in polymers and specific antibodies content. Immunoglobulin classes were also not affected by the same procedure.

Chromatography, Ion Exchange↗

PubMed1976

Nature of Escherichia coli mutants deficient in detergent-resistant and/or detergent-sensitive phospholipase A.

1. Escherichia coli K-12 mutants deficient in detergent-resistant (DR) and detergent-sensitive (DS) phospholipases A and deficient in DS phospholipase A were isolated. 2. The growth, compositions of phospholipids and fatty acids and turnover of phospholipids of three mutants (DR-, DS-, DR-DS-) were compared with those of their parent (DR- was isolated in a previous study). 3. Autodegradations of membrane phospholipids of 18,000 X g supernatants and precipitates of the homogenates of these three mutants were also compared with those of the parent, and the effects of various detergents and organic solvents on these activities were examined. 4. We could not identify any significant physiological role for DR or DS phospholipase A.

Detergents↗