PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10552850-6 1999 Plotting the changes in both Deltaepsilon(293) and [theta](205) against the loss of nativelike and sodium dodecyl sulfate-monomeric protein (assessed by polyacrylamide gel electrophoresis) showed a strong 1:1 relationship between Deltaepsilon(293) or [theta](205) and the loss of nativelike beta-Lg. Sodium Dodecyl Sulfate 99-121 beta-lactoglobulin Bos taurus 291-298 7766627-0 1995 Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine beta-lactoglobulin. Sodium Dodecyl Sulfate 10-32 beta-lactoglobulin Bos taurus 90-108 30615967-2 2019 The EGCG-modified beta-lg was characterized by SDS-PAGE, MALDI-TOF MS and intrinsic fluorescence spectroscopy. Sodium Dodecyl Sulfate 47-50 beta-lactoglobulin Bos taurus 18-25 1368553-4 1990 The recombinant met-beta-lactoglobulin migrated with the same molecular weight as native beta-lactoglobulin A on SDS-PAGE. Sodium Dodecyl Sulfate 113-116 beta-lactoglobulin Bos taurus 20-38 34106722-2 2021 Covalent modification of amino acids in BLG by flavonoids was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and o-phthaldialdehyde assay. Sodium Dodecyl Sulfate 75-97 beta-lactoglobulin Bos taurus 40-43 34106722-2 2021 Covalent modification of amino acids in BLG by flavonoids was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and o-phthaldialdehyde assay. Sodium Dodecyl Sulfate 134-137 beta-lactoglobulin Bos taurus 40-43 30615967-4 2019 SDS-PAGE and MALDI-TOF MS results indicated the dimerization of beta-lg after EGCG modification. Sodium Dodecyl Sulfate 0-3 beta-lactoglobulin Bos taurus 64-71 29428389-7 2018 Proteolysis of BLG, observed after sodium dodecyl sulfate-PAGE, was confirmed by the analysis of the peptide profiles by reversed-phase HPLC. Sodium Dodecyl Sulfate 35-57 beta-lactoglobulin Bos taurus 15-18 30030721-5 2019 Based on SDS-PAGE, HPLC analysis, and competitive ELISA, the reduction of disulfide bonds of BLG with OsNTRB/OsTrx23, OsNTRB/OsTrx1, GSH/OsTrx1, or GSH/OsTrx20 increased its trypsin digestibility and reduced its immunoreactivity. Sodium Dodecyl Sulfate 9-12 beta-lactoglobulin Bos taurus 93-96 25450833-6 2015 ITC studies showed that at pH 7.5 GLG binds sodium dodecyl sulfate with Gibbs energy similar to BLG, however, with different contribution from enthalpic and entropic component. Sodium Dodecyl Sulfate 44-66 beta-lactoglobulin Bos taurus 34-37 26281976-5 2015 The purity and native like folded structure of the recombinant Lys69Asn beta-LG was confirmed by HPLC, SDS-PAGE, mass spectrometry and circular dichroism. Sodium Dodecyl Sulfate 103-106 beta-lactoglobulin Bos taurus 72-79 27047145-6 2015 Molecular weight of the purified cattle beta-lg was determined by 15 percent one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis and was analyzed by gel documentation system using standard molecular weight marker. Sodium Dodecyl Sulfate 93-115 beta-lactoglobulin Bos taurus 40-47 25315246-3 2015 Conjugation between BLG and each SSPS was confirmed by Sodium dodecyl sulfate polyacrylamide gel electrophoresis and isoelectric focusing. Sodium Dodecyl Sulfate 55-77 beta-lactoglobulin Bos taurus 20-23 23498006-5 2013 Furthermore, the molecular weight of beta-LG increased from 18.4 to 19.9 kDa after conjugation with FOS, as evaluated by sodium dodecyl sulfate-PAGE and mass spectrometry. Sodium Dodecyl Sulfate 121-143 beta-lactoglobulin Bos taurus 37-44 21108136-5 2010 Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) suggested that beta-LG was purified to apparent homogeneity, while absorption, fluorescence, and circular dichroism spectroscopy indicated the native-like conformation of the protein. Sodium Dodecyl Sulfate 0-22 beta-lactoglobulin Bos taurus 84-91 20723666-5 2010 After treatment with gastrointestinal pH and digestive enzymes, beta-LG-CLA complex showed very good stability in gastrointestinal conditions in vitro, measured by zeta potential analyzer and sodium dodecyl sulfate PAGE, respectively. Sodium Dodecyl Sulfate 192-214 beta-lactoglobulin Bos taurus 64-71 21108136-5 2010 Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) suggested that beta-LG was purified to apparent homogeneity, while absorption, fluorescence, and circular dichroism spectroscopy indicated the native-like conformation of the protein. Sodium Dodecyl Sulfate 59-62 beta-lactoglobulin Bos taurus 84-91 16554059-5 2006 The formation of non-native alpha-helical intermediate of thiol modified beta-lactoglobulin (TNB-beta-LG) was induced by n-alkyl sulfates including sodium octyl sulfate, SOS; sodium decyl sulfate, SDeS; sodium dodecyl sulfate, SDS; and sodium tetradecyl sulfate, STS at pH 7.5 and 2. Sodium Dodecyl Sulfate 203-225 beta-lactoglobulin Bos taurus 73-91 18698816-0 2008 Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate. Sodium Dodecyl Sulfate 81-103 beta-lactoglobulin Bos taurus 26-44 18698816-1 2008 We report on the conformation of heat-induced bovine beta-lactoglobulin (betalg) aggregates prepared at different pH conditions, and their complexes with model anionic surfactants such as sodium dodecyl sulfate (SDS). Sodium Dodecyl Sulfate 188-210 beta-lactoglobulin Bos taurus 53-71 18698816-1 2008 We report on the conformation of heat-induced bovine beta-lactoglobulin (betalg) aggregates prepared at different pH conditions, and their complexes with model anionic surfactants such as sodium dodecyl sulfate (SDS). Sodium Dodecyl Sulfate 212-215 beta-lactoglobulin Bos taurus 53-71 18680375-2 2008 To elucidate the still unknown structure-function relationship in this protein, the structural changes of beta-lactoglobulin variant A (beta-LG A) in the presence of anionic surfactant such as sodium n-dodecyl sulfate (SDS) and in the presence of nonionic surfactant such as Triton X-100 have been investigated. Sodium Dodecyl Sulfate 193-217 beta-lactoglobulin Bos taurus 136-143 18680375-2 2008 To elucidate the still unknown structure-function relationship in this protein, the structural changes of beta-lactoglobulin variant A (beta-LG A) in the presence of anionic surfactant such as sodium n-dodecyl sulfate (SDS) and in the presence of nonionic surfactant such as Triton X-100 have been investigated. Sodium Dodecyl Sulfate 219-222 beta-lactoglobulin Bos taurus 106-124 18680375-4 2008 The results of UV-vis and fluorescence studies show a higher denaturating effect of SDS at acid pH that can be due to greater positive charges of beta-LG at this pH indicating also the nonspecific hydrophobic interactions of Triton X-100 with beta-LG at all studied pHs. Sodium Dodecyl Sulfate 84-87 beta-lactoglobulin Bos taurus 146-153 18680375-4 2008 The results of UV-vis and fluorescence studies show a higher denaturating effect of SDS at acid pH that can be due to greater positive charges of beta-LG at this pH indicating also the nonspecific hydrophobic interactions of Triton X-100 with beta-LG at all studied pHs. Sodium Dodecyl Sulfate 84-87 beta-lactoglobulin Bos taurus 243-250 17708643-4 2007 RP-HPLC-UV, SDS-PAGE, and IEF profiles of beta-LG were modified as a consequence of its glycation. Sodium Dodecyl Sulfate 12-15 beta-lactoglobulin Bos taurus 42-49 16554059-5 2006 The formation of non-native alpha-helical intermediate of thiol modified beta-lactoglobulin (TNB-beta-LG) was induced by n-alkyl sulfates including sodium octyl sulfate, SOS; sodium decyl sulfate, SDeS; sodium dodecyl sulfate, SDS; and sodium tetradecyl sulfate, STS at pH 7.5 and 2. Sodium Dodecyl Sulfate 203-225 beta-lactoglobulin Bos taurus 97-104 16554059-5 2006 The formation of non-native alpha-helical intermediate of thiol modified beta-lactoglobulin (TNB-beta-LG) was induced by n-alkyl sulfates including sodium octyl sulfate, SOS; sodium decyl sulfate, SDeS; sodium dodecyl sulfate, SDS; and sodium tetradecyl sulfate, STS at pH 7.5 and 2. Sodium Dodecyl Sulfate 227-230 beta-lactoglobulin Bos taurus 73-91 16554059-5 2006 The formation of non-native alpha-helical intermediate of thiol modified beta-lactoglobulin (TNB-beta-LG) was induced by n-alkyl sulfates including sodium octyl sulfate, SOS; sodium decyl sulfate, SDeS; sodium dodecyl sulfate, SDS; and sodium tetradecyl sulfate, STS at pH 7.5 and 2. Sodium Dodecyl Sulfate 227-230 beta-lactoglobulin Bos taurus 97-104 16190664-0 2005 Influence of binding of sodium dodecyl sulfate, all-trans-retinol, and 8-anilino-1-naphthalenesulfonate on the high-pressure-induced unfolding and aggregation of beta-lactoglobulin B. Sodium Dodecyl Sulfate 24-46 beta-lactoglobulin Bos taurus 162-182 16009637-4 2005 Albumin bovine, beta-lactoglobulin and alpha-lactalbumin from whey solutions in the presence of sodium dodecyl sulfate could be transferred into the foam fraction with enrichment ratios of up to 30 and with recovery rates between 64.5% and 99.8%. Sodium Dodecyl Sulfate 96-118 beta-lactoglobulin Bos taurus 16-34 12350100-2 2002 Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis under non-reducing and reducing conditions showed that in the early stages of the aggregation of beta-lactoglobulin disulfide linked aggregates were formed on heating at pH 6.7, but not at pH 4.9. Sodium Dodecyl Sulfate 0-23 beta-lactoglobulin Bos taurus 176-194 12484782-2 2002 The stability of BLG against unfolding is sharply affected by the pH of the medium: both A and B BLG variants are maximally stabilized against urea denaturation at acidic pH and against SDS denaturation at alkaline pH. Sodium Dodecyl Sulfate 186-189 beta-lactoglobulin Bos taurus 17-20 12484782-2 2002 The stability of BLG against unfolding is sharply affected by the pH of the medium: both A and B BLG variants are maximally stabilized against urea denaturation at acidic pH and against SDS denaturation at alkaline pH. Sodium Dodecyl Sulfate 186-189 beta-lactoglobulin Bos taurus 97-100 15826078-0 2005 Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of beta-lactoglobulin B. Sodium Dodecyl Sulfate 24-46 beta-lactoglobulin Bos taurus 164-184 15826078-4 2005 Both palmitate and SDS stabilized the native structure of beta-LG against heat-induced structural flexibility, subsequent unfolding, and denaturation. Sodium Dodecyl Sulfate 19-22 beta-lactoglobulin Bos taurus 58-65 15826078-6 2005 It was also noted that holding a beta-LG solution with added SDS or ANS promoted the formation of a hydrophobically associated non-native dimer. Sodium Dodecyl Sulfate 61-64 beta-lactoglobulin Bos taurus 33-40 12350100-2 2002 Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis under non-reducing and reducing conditions showed that in the early stages of the aggregation of beta-lactoglobulin disulfide linked aggregates were formed on heating at pH 6.7, but not at pH 4.9. Sodium Dodecyl Sulfate 60-63 beta-lactoglobulin Bos taurus 176-194 12350100-9 2002 The combination of SDS-PAGE and MALDI-TOF MS enables us to understand the mechanism of beta-lactoglobulin aggregation at the macromolecular level. Sodium Dodecyl Sulfate 19-22 beta-lactoglobulin Bos taurus 87-105 11851426-3 2002 For the peptide fragment covering the more flexible N-terminal region of BLG (beta-strands A, B), where both theoretical predictions and kinetic refolding experiments suggested the formation of non-native alpha-helix, no native long-range contacts were identified, and a helical secondary structure was stabilized only in the presence of 25 mM SDS. Sodium Dodecyl Sulfate 344-347 beta-lactoglobulin Bos taurus 73-76