PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10099536-6 1999 Polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS-PAGE) was used to quantify the separation of lysozyme from ribonuclease, alkaline phosphatase from insulin, and trypsin from catalase. Sodium Dodecyl Sulfate 38-60 lysozyme Homo sapiens 111-119 10667860-2 2000 The interaction between Lyso, Triton X-100 and SDS micelles was quantified by determining the respective associations constant (K(Lyso)). Sodium Dodecyl Sulfate 47-50 lysozyme Homo sapiens 24-28 10667860-2 2000 The interaction between Lyso, Triton X-100 and SDS micelles was quantified by determining the respective associations constant (K(Lyso)). Sodium Dodecyl Sulfate 47-50 lysozyme Homo sapiens 130-134 10667860-3 2000 Values were 37 M(-1) for Triton X-100 and 514 M(-1) for SDS, indicating that the Lyso molecule binds Triton X-100 micelles effectively and SDS micelles even more strongly. Sodium Dodecyl Sulfate 56-59 lysozyme Homo sapiens 81-85 10667860-3 2000 Values were 37 M(-1) for Triton X-100 and 514 M(-1) for SDS, indicating that the Lyso molecule binds Triton X-100 micelles effectively and SDS micelles even more strongly. Sodium Dodecyl Sulfate 139-142 lysozyme Homo sapiens 81-85 10667860-6 2000 The results indicate that the O2 (1deltag) attack on the interior of Lyso on amino acid residues, was more effective in leading to a photo-oxidative reaction in SDS and in Triton X-100 at surfactant concentrations < 1 x 10(-2) M than in a homogeneous solution. Sodium Dodecyl Sulfate 161-164 lysozyme Homo sapiens 69-73 11134973-2 2001 Oxidative refolding and thermal unfolding of ribonuclease A, lysozyme, and protein disulfide isomerase led to the formation of cross-linked dimers/oligomers as revealed by SDS-polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 172-175 lysozyme Homo sapiens 61-69 10099536-6 1999 Polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS-PAGE) was used to quantify the separation of lysozyme from ribonuclease, alkaline phosphatase from insulin, and trypsin from catalase. Sodium Dodecyl Sulfate 62-65 lysozyme Homo sapiens 111-119 10063615-6 1999 The recombinant protein produced was actually shown to be the human lysozyme, using renaturing SDS-PAGE and Western blot techniques. Sodium Dodecyl Sulfate 95-98 lysozyme Homo sapiens 68-76 12555402-1 1999 To obtain the SDS-PAGE-pure human lysozyme, the crude enzyme of engineered bacterium E. coli was purified by chromatography on cation ion exchange of Express-Ion S. The optimum reaction temperature and pH of this lysozyme were 45 degrees C and 6.5, respectively. Sodium Dodecyl Sulfate 14-17 lysozyme Homo sapiens 34-42 12555402-1 1999 To obtain the SDS-PAGE-pure human lysozyme, the crude enzyme of engineered bacterium E. coli was purified by chromatography on cation ion exchange of Express-Ion S. The optimum reaction temperature and pH of this lysozyme were 45 degrees C and 6.5, respectively. Sodium Dodecyl Sulfate 14-17 lysozyme Homo sapiens 213-221 18966619-1 1996 The use of Cresyl Violet and sodium dodecyl sulphate for the kinetic fluorimetric determination of lysozyme from dynamic fluorescence measurements at a long wavelength in the range near 600 nm was explored. Sodium Dodecyl Sulfate 29-52 lysozyme Homo sapiens 99-107 9795050-10 1998 The greater amount of additional lysozyme release by sodium dodecyl sulfate than by guanidine hydrochloride suggested that protein surface adsorption was a more critical factor in protein release than aggregation. Sodium Dodecyl Sulfate 53-75 lysozyme Homo sapiens 33-41 8175140-3 1994 The production and modulation of lysozyme synthesis was studied by means of Northern-blot analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and a specific bioassay after treatment of the cells with interleukin-1 beta, interleukin-6 and tumor necrosis factor-alpha. Sodium Dodecyl Sulfate 100-122 lysozyme Homo sapiens 33-41 8218378-6 1993 with a yield of 6.5 mol OH./mol lysozyme; moreover, SDS-PAGE showed a loss of native lysozyme (14.4 kDa), the presence of dimer and trimer aggregates and characteristic fragmentation. Sodium Dodecyl Sulfate 52-55 lysozyme Homo sapiens 85-93 34908081-7 2022 At low S/Ps (0 <= S/P <= 10), the SDS concentration is not enough to fully neutralize the charge of lysozyme, leading to the formation of cationic SDS-lysozyme complex-mediated nanoparticle aggregation. Sodium Dodecyl Sulfate 147-150 lysozyme Homo sapiens 151-159 1516730-11 1992 Bronchial lysozyme was also denatured by sodium dodecyl sulphate. Sodium Dodecyl Sulfate 41-64 lysozyme Homo sapiens 10-18 34908081-7 2022 At low S/Ps (0 <= S/P <= 10), the SDS concentration is not enough to fully neutralize the charge of lysozyme, leading to the formation of cationic SDS-lysozyme complex-mediated nanoparticle aggregation. Sodium Dodecyl Sulfate 147-150 lysozyme Homo sapiens 100-108 2040307-7 1991 Our results suggest that the de novo synthesized products reflect the conformational states in vivo to some extent, and that the formation of SDS-resistant compact conformation can be regarded as a necessary condition for allowing lysozyme to be secreted. Sodium Dodecyl Sulfate 142-145 lysozyme Homo sapiens 231-239 34908081-0 2022 Tuning of silica nanoparticle-lysozyme protein complexes in the presence of the SDS surfactant. Sodium Dodecyl Sulfate 80-83 lysozyme Homo sapiens 30-38 34908081-1 2022 The structures of the complexes of anionic silica nanoparticle (size ~ 16 nm)-lysozyme (cationic) protein, tuned by the addition of the anionic surfactant sodium dodecyl sulfate (SDS), have been investigated by dynamic light scattering (DLS) and small-angle neutron scattering (SANS). Sodium Dodecyl Sulfate 155-177 lysozyme Homo sapiens 78-86 34908081-1 2022 The structures of the complexes of anionic silica nanoparticle (size ~ 16 nm)-lysozyme (cationic) protein, tuned by the addition of the anionic surfactant sodium dodecyl sulfate (SDS), have been investigated by dynamic light scattering (DLS) and small-angle neutron scattering (SANS). Sodium Dodecyl Sulfate 179-182 lysozyme Homo sapiens 78-86 34908081-4 2022 The presence of SDS, however, remarkably affects the nanoparticle-protein interactions via binding with the oppositely charged segments of lysozyme. Sodium Dodecyl Sulfate 16-19 lysozyme Homo sapiens 139-147 34908081-5 2022 In general, the SDS-lysozyme complexes possess a variety of structures (e.g., insoluble complexes of Ly(DS)8, crystalline structure, or micelle-like structure) depending on the surfactant-to-protein molar ratio (S/P). Sodium Dodecyl Sulfate 16-19 lysozyme Homo sapiens 20-28 34908081-6 2022 In the ternary system (HS40-lysozyme-SDS), lysozyme preferentially binds with SDS, instead of directly to nanoparticles. Sodium Dodecyl Sulfate 37-40 lysozyme Homo sapiens 28-36 34908081-6 2022 In the ternary system (HS40-lysozyme-SDS), lysozyme preferentially binds with SDS, instead of directly to nanoparticles. Sodium Dodecyl Sulfate 37-40 lysozyme Homo sapiens 43-51 34908081-6 2022 In the ternary system (HS40-lysozyme-SDS), lysozyme preferentially binds with SDS, instead of directly to nanoparticles. Sodium Dodecyl Sulfate 78-81 lysozyme Homo sapiens 28-36 34908081-6 2022 In the ternary system (HS40-lysozyme-SDS), lysozyme preferentially binds with SDS, instead of directly to nanoparticles. Sodium Dodecyl Sulfate 78-81 lysozyme Homo sapiens 43-51 34908081-7 2022 At low S/Ps (0 <= S/P <= 10), the SDS concentration is not enough to fully neutralize the charge of lysozyme, leading to the formation of cationic SDS-lysozyme complex-mediated nanoparticle aggregation. Sodium Dodecyl Sulfate 34-37 lysozyme Homo sapiens 100-108 34908081-7 2022 At low S/Ps (0 <= S/P <= 10), the SDS concentration is not enough to fully neutralize the charge of lysozyme, leading to the formation of cationic SDS-lysozyme complex-mediated nanoparticle aggregation. Sodium Dodecyl Sulfate 34-37 lysozyme Homo sapiens 151-159 34908081-8 2022 The morphology of the nanoparticle-(lysozyme-SDS) complexes is also found to be mass fractal kind where the fractal dimension increases with increasing SDS concentration. Sodium Dodecyl Sulfate 45-48 lysozyme Homo sapiens 36-44 34908081-8 2022 The morphology of the nanoparticle-(lysozyme-SDS) complexes is also found to be mass fractal kind where the fractal dimension increases with increasing SDS concentration. Sodium Dodecyl Sulfate 152-155 lysozyme Homo sapiens 36-44 34908081-9 2022 At S/P > 10, there is sufficient SDS to fully neutralize the lysozyme in the absence of competing charges from the particle but it is at S/P = 50 before all lysozyme desorbs from the particle and binds completely to the overwhelming amount of SDS, creating an oppositely charged lysozyme-SDS complex, which is repelled from the particle. Sodium Dodecyl Sulfate 33-36 lysozyme Homo sapiens 61-69 34908081-9 2022 At S/P > 10, there is sufficient SDS to fully neutralize the lysozyme in the absence of competing charges from the particle but it is at S/P = 50 before all lysozyme desorbs from the particle and binds completely to the overwhelming amount of SDS, creating an oppositely charged lysozyme-SDS complex, which is repelled from the particle. Sodium Dodecyl Sulfate 243-246 lysozyme Homo sapiens 61-69 34908081-9 2022 At S/P > 10, there is sufficient SDS to fully neutralize the lysozyme in the absence of competing charges from the particle but it is at S/P = 50 before all lysozyme desorbs from the particle and binds completely to the overwhelming amount of SDS, creating an oppositely charged lysozyme-SDS complex, which is repelled from the particle. Sodium Dodecyl Sulfate 243-246 lysozyme Homo sapiens 157-165 34908081-9 2022 At S/P > 10, there is sufficient SDS to fully neutralize the lysozyme in the absence of competing charges from the particle but it is at S/P = 50 before all lysozyme desorbs from the particle and binds completely to the overwhelming amount of SDS, creating an oppositely charged lysozyme-SDS complex, which is repelled from the particle. Sodium Dodecyl Sulfate 288-291 lysozyme Homo sapiens 157-165 3190458-2 1988 Rat LZM which showed a single protein band on sodium dodecylsulfate polyacrylamide gel electrophoresis was purified by ion-exchange chromatography and gel filtration. Sodium Dodecyl Sulfate 46-67 lysozyme Homo sapiens 4-7 3223094-0 1988 Determination of lysozyme content in eggs and egg products using SDS-gel electrophoresis. Sodium Dodecyl Sulfate 65-68 lysozyme Homo sapiens 17-25 2706941-0 1989 Lysozyme activity in animal extracts after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 43-65 lysozyme Homo sapiens 0-8 2706941-2 1989 Lysozyme activity was detected after electrophoresis in sodium dodecyl sulfate-polyacrylamide gels containing 0.2% (W/V) autoclaved Micrococcus lysodeikticus cells as substrate. Sodium Dodecyl Sulfate 56-78 lysozyme Homo sapiens 0-8 30504623-3 2018 SDS-PAGE showed that photocatalysis with g-STO:Rh induced the fragmentation of lysozyme into unidentifiable decomposition products. Sodium Dodecyl Sulfate 0-3 lysozyme Homo sapiens 79-87 7322122-0 1981 [The mechanism of binding of sodium dodecyl sulfate by lysozyme]. Sodium Dodecyl Sulfate 29-51 lysozyme Homo sapiens 55-63 32028858-4 2021 The calculated values were found to decrease with increasing SDS concentration in the BSA solutions, but to increase with SDS concentration in the LYZ solutions. Sodium Dodecyl Sulfate 122-125 lysozyme Homo sapiens 147-150 30665033-4 2019 In this paper, we report our investigation on lysozyme modifications upon treatment with selected benzoquinones (BQs), utilizing fluorescence spectroscopy including anisotropy determination, UV-Vis spectroscopy, and SDS-PAGE. Sodium Dodecyl Sulfate 216-219 lysozyme Homo sapiens 46-54 2424976-3 1986 LZM was identified by the capacity of cell lysates or medium to lyse Micrococcus lysodeikticus, and by the presence of a 14.5 Kd protein band which co-migrated with human LZM in SDS-PAGE and which reacted positively in Western blots with antiserum to human LZM. Sodium Dodecyl Sulfate 178-181 lysozyme Homo sapiens 0-3 2424976-3 1986 LZM was identified by the capacity of cell lysates or medium to lyse Micrococcus lysodeikticus, and by the presence of a 14.5 Kd protein band which co-migrated with human LZM in SDS-PAGE and which reacted positively in Western blots with antiserum to human LZM. Sodium Dodecyl Sulfate 178-181 lysozyme Homo sapiens 171-174 2424976-3 1986 LZM was identified by the capacity of cell lysates or medium to lyse Micrococcus lysodeikticus, and by the presence of a 14.5 Kd protein band which co-migrated with human LZM in SDS-PAGE and which reacted positively in Western blots with antiserum to human LZM. Sodium Dodecyl Sulfate 178-181 lysozyme Homo sapiens 171-174 33278495-7 2021 Lysozyme entrapped in microneedles was characterized using circular dichroism and SDS-page analysis for structural stability post microneedle fabrication. Sodium Dodecyl Sulfate 82-85 lysozyme Homo sapiens 0-8 30504623-9 2018 Lysozyme was denatured more quickly by g-STO:Rh/Sb photocatalysis than by g-STO:Rh according to analysis by SDS-PAGE, CD spectroscopy, BCA and Bradford protein assays, and lytic activity. Sodium Dodecyl Sulfate 108-111 lysozyme Homo sapiens 0-8 26308474-0 2015 Unfolding and folding pathway of lysozyme induced by sodium dodecyl sulfate. Sodium Dodecyl Sulfate 53-75 lysozyme Homo sapiens 33-41 27768744-0 2016 Molecular Insight into Human Lysozyme and Its Ability to Form Amyloid Fibrils in High Concentrations of Sodium Dodecyl Sulfate: A View from Molecular Dynamics Simulations. Sodium Dodecyl Sulfate 104-126 lysozyme Homo sapiens 29-37 27768744-4 2016 In this study, we conducted two 500000 ps molecular dynamics (MD) simulations of human lysozyme in sodium dodecyl sulfate (SDS) at two ambient temperatures. Sodium Dodecyl Sulfate 99-121 lysozyme Homo sapiens 87-95 27768744-4 2016 In this study, we conducted two 500000 ps molecular dynamics (MD) simulations of human lysozyme in sodium dodecyl sulfate (SDS) at two ambient temperatures. Sodium Dodecyl Sulfate 123-126 lysozyme Homo sapiens 87-95 27768744-6 2016 The aim of this study was to provide further molecular insight into all interactions in the lysozyme-SDS complexes and to provide a perspective on the ability of human lysozyme to form amyloid fibrils in the presence of SDS surfactant molecules. Sodium Dodecyl Sulfate 101-104 lysozyme Homo sapiens 92-100 27768744-6 2016 The aim of this study was to provide further molecular insight into all interactions in the lysozyme-SDS complexes and to provide a perspective on the ability of human lysozyme to form amyloid fibrils in the presence of SDS surfactant molecules. Sodium Dodecyl Sulfate 101-104 lysozyme Homo sapiens 168-176 27768744-6 2016 The aim of this study was to provide further molecular insight into all interactions in the lysozyme-SDS complexes and to provide a perspective on the ability of human lysozyme to form amyloid fibrils in the presence of SDS surfactant molecules. Sodium Dodecyl Sulfate 220-223 lysozyme Homo sapiens 168-176 27768744-10 2016 Therefore, we suggest that future studies investigate the beta-amyloid formation of human lysozyme at SDS concentrations above the CMC and at high temperatures. Sodium Dodecyl Sulfate 102-105 lysozyme Homo sapiens 90-98 27375592-8 2016 Transmission electron microscopy (TEM) and SDS-PAGE showed tear fluid and lysozyme-induced OMVs were similar in size and protein composition, but differed from biofilm-harvested OMVs, the latter smaller with fewer proteins. Sodium Dodecyl Sulfate 43-46 lysozyme Homo sapiens 74-82 26197052-5 2015 The radical yields were estimated and the lysozyme modifications were analyzed by SDS-PAGE, western blot, enzymatic activity and MS/MS analysis. Sodium Dodecyl Sulfate 82-85 lysozyme Homo sapiens 42-50 26308474-2 2015 In the present study, the unfolding and folding pathway of hen egg white lysozyme (HEWL) induced by sodium dodecyl sulfate (SDS) is studied. Sodium Dodecyl Sulfate 100-122 lysozyme Homo sapiens 73-81 26308474-2 2015 In the present study, the unfolding and folding pathway of hen egg white lysozyme (HEWL) induced by sodium dodecyl sulfate (SDS) is studied. Sodium Dodecyl Sulfate 124-127 lysozyme Homo sapiens 73-81 24128540-8 2014 Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results showed that the purity of the obtained lysozyme was ~80.7% and that the recovery yield was ~89.1%. Sodium Dodecyl Sulfate 0-22 lysozyme Homo sapiens 116-124 25577059-5 2015 The results of SDS-PAGE patterns indicated that lysozyme was prone to precipitate, and was relatively the higher component of aggregates. Sodium Dodecyl Sulfate 15-18 lysozyme Homo sapiens 48-56 32261784-2 2014 The PNIPAM-b-LCP/SDS-functionalized 5CB droplets were effective in detecting proteins in water through a radial-to-bipolar (R-B) orientational change, with detection limits of 0.95, 1.1, 0.12, and 0.07 muM for bovine serum albumin (BSA), lysozyme (LYZ), hemoglobin (Hb), and chymotrypsinogen (ChTg), respectively. Sodium Dodecyl Sulfate 17-20 lysozyme Homo sapiens 238-246 32261784-2 2014 The PNIPAM-b-LCP/SDS-functionalized 5CB droplets were effective in detecting proteins in water through a radial-to-bipolar (R-B) orientational change, with detection limits of 0.95, 1.1, 0.12, and 0.07 muM for bovine serum albumin (BSA), lysozyme (LYZ), hemoglobin (Hb), and chymotrypsinogen (ChTg), respectively. Sodium Dodecyl Sulfate 17-20 lysozyme Homo sapiens 248-251 24647567-0 2014 Protonation favors aggregation of lysozyme with SDS. Sodium Dodecyl Sulfate 48-51 lysozyme Homo sapiens 34-42 24647567-5 2014 Negatively charged SDS was used to "antagonize" positive charges on lysozyme. Sodium Dodecyl Sulfate 19-22 lysozyme Homo sapiens 68-76 24647567-6 2014 We examined the effects of pH variations on SDS-induced amyloid fibril formation by lysozyme using methods such as far-UV circular dichroism, Rayleigh scattering, turbidity measurements, dye binding assays and dynamic light scattering. Sodium Dodecyl Sulfate 44-47 lysozyme Homo sapiens 84-92 24647567-7 2014 We found that sub-micellar concentrations of SDS (0.1 to 0.6 mM) induced amyloid fibril formation by lysozyme in the pH range of 10.0-1.0 and maximum aggregation was observed at pH 1.0. Sodium Dodecyl Sulfate 45-48 lysozyme Homo sapiens 101-109 24128540-8 2014 Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results showed that the purity of the obtained lysozyme was ~80.7% and that the recovery yield was ~89.1%. Sodium Dodecyl Sulfate 59-62 lysozyme Homo sapiens 116-124 22405581-2 2012 Analysis of the process by means of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) revealed that the complexes are formed by sequential adsorption of ovotransferrin, ovalbumins, ovomucoid and lysozyme on the surface of the silicate. Sodium Dodecyl Sulfate 95-98 lysozyme Homo sapiens 214-222 23110666-0 2012 Secondary structural changes of homologous proteins, lysozyme and alpha-lactalbumin, in thermal denaturation up to 130 C and sodium dodecyl sulfate (SDS) effects on these changes: comparison of thermal stabilities of SDS-induced helical structures in these proteins. Sodium Dodecyl Sulfate 126-148 lysozyme Homo sapiens 53-61 23110666-4 2012 All of the SDS-induced helices of lysozyme were disrupted below 60 C, while those of alpha-lactalbumin at 10 mM SDS were unchanged up to 130 C. A similarity was also fixed. Sodium Dodecyl Sulfate 11-14 lysozyme Homo sapiens 34-42 25359082-5 2014 RESULTS: The SDS-PAGE pattern of LYS treated with papain under nonreducing conditions showed the presence of intact LYS that partially disappeared following reduction with beta-mercaptoethanol, releasing IgE-reactive fragments as determined by Western blotting. Sodium Dodecyl Sulfate 13-16 lysozyme Homo sapiens 33-36 25359082-5 2014 RESULTS: The SDS-PAGE pattern of LYS treated with papain under nonreducing conditions showed the presence of intact LYS that partially disappeared following reduction with beta-mercaptoethanol, releasing IgE-reactive fragments as determined by Western blotting. Sodium Dodecyl Sulfate 13-16 lysozyme Homo sapiens 116-119 12128183-1 2002 I. Microcalorimetric investigation on the interaction of cetyltrimethylammonium bromide (CTAB) and sodium dodecylsulfate (SDS) with gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA). Sodium Dodecyl Sulfate 99-120 lysozyme Homo sapiens 146-154 22146703-9 2012 Lactoferrin and lysozyme showed antibacterial and bacteriolytic activity, which was abolished after SDS treatment; this loss of activity did not occur for proteins treated with iMPS. Sodium Dodecyl Sulfate 100-103 lysozyme Homo sapiens 16-24 22146703-10 2012 CONCLUSIONS: These data clearly show that the iMPS prevents the denaturation of physiologic levels of human lactoferrin and lysozyme by the strongly denaturing surfactant SDS and that stabilized proteins retain their function. Sodium Dodecyl Sulfate 171-174 lysozyme Homo sapiens 124-132 17889513-0 2008 A direct calorimetric determination of denaturation enthalpy for lysozyme in sodium dodecyl sulfate. Sodium Dodecyl Sulfate 77-99 lysozyme Homo sapiens 65-73 17889513-1 2008 Thermodynamics of the interaction between sodium dodecyl sulfate (SDS) with lysozyme were investigated at pH 7.0 and 27 degrees C in phosphate buffer by isothermal titration calorimetry. Sodium Dodecyl Sulfate 42-64 lysozyme Homo sapiens 76-84 17889513-1 2008 Thermodynamics of the interaction between sodium dodecyl sulfate (SDS) with lysozyme were investigated at pH 7.0 and 27 degrees C in phosphate buffer by isothermal titration calorimetry. Sodium Dodecyl Sulfate 66-69 lysozyme Homo sapiens 76-84 17889513-3 2008 The new solvation model was used to reproduce the enthalpies of lysozyme-SDS interaction over the whole range of SDS concentrations. Sodium Dodecyl Sulfate 73-76 lysozyme Homo sapiens 64-72 17889513-3 2008 The new solvation model was used to reproduce the enthalpies of lysozyme-SDS interaction over the whole range of SDS concentrations. Sodium Dodecyl Sulfate 113-116 lysozyme Homo sapiens 64-72 17889513-5 2008 At low concentrations of SDS, the binding is mainly electrostatic, with some simultaneous interaction of the hydrophobic tail with nearby hydrophobic patches on the lysozyme. Sodium Dodecyl Sulfate 25-28 lysozyme Homo sapiens 165-173 17616361-0 2007 Fibril formation of lysozyme upon interaction with sodium dodecyl sulfate at pH 9.2. Sodium Dodecyl Sulfate 51-73 lysozyme Homo sapiens 20-28 17616361-3 2007 This paper studies the interaction of lysozyme with sodium dodecyl sulfate (SDS) at pH 9.2, using UV-visible spectrophotometry, circular dichroism (CD) spectropolarimetry, electron microscopy (EM) and chemometry. Sodium Dodecyl Sulfate 52-74 lysozyme Homo sapiens 38-46 17616361-3 2007 This paper studies the interaction of lysozyme with sodium dodecyl sulfate (SDS) at pH 9.2, using UV-visible spectrophotometry, circular dichroism (CD) spectropolarimetry, electron microscopy (EM) and chemometry. Sodium Dodecyl Sulfate 76-79 lysozyme Homo sapiens 38-46 17616361-4 2007 Based on observations such as the strange increase in absorbance at 650nm (pH 9.2) and the presence of intermediates, it is assumed that lysozyme fibrils have been formed at pH 9.2 in the presence of SDS as an anionic surfactant. Sodium Dodecyl Sulfate 200-203 lysozyme Homo sapiens 137-145 16013553-4 2005 This result was confirmed by non-reducing sodium dodecyl sulfate-polyacrylamide gel electrohoresis (SDS-PAGE) analysis of renatured lysozyme molecules with the dilution method. Sodium Dodecyl Sulfate 42-64 lysozyme Homo sapiens 132-140 16013553-4 2005 This result was confirmed by non-reducing sodium dodecyl sulfate-polyacrylamide gel electrohoresis (SDS-PAGE) analysis of renatured lysozyme molecules with the dilution method. Sodium Dodecyl Sulfate 100-103 lysozyme Homo sapiens 132-140 12772737-2 2003 METHODS: After extraction, lysozyme concentration in each extract was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. Sodium Dodecyl Sulfate 84-106 lysozyme Homo sapiens 27-35 12772737-2 2003 METHODS: After extraction, lysozyme concentration in each extract was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. Sodium Dodecyl Sulfate 143-146 lysozyme Homo sapiens 27-35 12128183-1 2002 I. Microcalorimetric investigation on the interaction of cetyltrimethylammonium bromide (CTAB) and sodium dodecylsulfate (SDS) with gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA). Sodium Dodecyl Sulfate 99-120 lysozyme Homo sapiens 156-158 12128183-1 2002 I. Microcalorimetric investigation on the interaction of cetyltrimethylammonium bromide (CTAB) and sodium dodecylsulfate (SDS) with gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA). Sodium Dodecyl Sulfate 122-125 lysozyme Homo sapiens 146-154 12128183-1 2002 I. Microcalorimetric investigation on the interaction of cetyltrimethylammonium bromide (CTAB) and sodium dodecylsulfate (SDS) with gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA). Sodium Dodecyl Sulfate 122-125 lysozyme Homo sapiens 156-158 12128183-2 2002 The interaction of the surfactants cetyltrimethyl ammonium bromide (CTAB) and sodium dodecyl sulfate (SDS) with the biopolymers gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA) was studied by isothermal titration microcalorimetry at varied biopolymer concentration, pH and temperature. Sodium Dodecyl Sulfate 78-100 lysozyme Homo sapiens 142-150 12128183-2 2002 The interaction of the surfactants cetyltrimethyl ammonium bromide (CTAB) and sodium dodecyl sulfate (SDS) with the biopolymers gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA) was studied by isothermal titration microcalorimetry at varied biopolymer concentration, pH and temperature. Sodium Dodecyl Sulfate 102-105 lysozyme Homo sapiens 142-150