PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15043949-6 2004 SDS-PAGE, N-terminal sequence and mass spectrometric analysis demonstrated the high degree of purity and expected molecular masses of the three C3a molecules. Sodium Dodecyl Sulfate 0-3 complement C3 Homo sapiens 144-147 15921941-5 2005 SDS-PAGE, followed by Western blot analysis, revealed the presence of two alligator serum proteins with nearly identical molecular weights as human C3alpha and C3beta. Sodium Dodecyl Sulfate 0-3 complement C3 Homo sapiens 148-155 10698338-6 1999 These complexes are detected on SDS-PAGE by two bands of molecular composition, C3alpha65-C3alpha43 (band A) and C3alpha65-heavy chain of the Ab (band B), which correspond to C3b-C3b and C3b-IgG covalent interaction respectively, and that identify opsonized IC (C3b-IC). Sodium Dodecyl Sulfate 32-35 complement C3 Homo sapiens 175-178 11447230-2 2001 Upon interaction of C3 with IgG.IC, C3b.C3b.IgG covalent complexes are formed that are detected on SDS-polyacrylamide gel electrophoresis by two bands corresponding to C3b.C3b (band A) and C3b.IgG (band B) covalent complexes. Sodium Dodecyl Sulfate 99-102 complement C3 Homo sapiens 36-39 11447230-2 2001 Upon interaction of C3 with IgG.IC, C3b.C3b.IgG covalent complexes are formed that are detected on SDS-polyacrylamide gel electrophoresis by two bands corresponding to C3b.C3b (band A) and C3b.IgG (band B) covalent complexes. Sodium Dodecyl Sulfate 99-102 complement C3 Homo sapiens 40-43 11447230-2 2001 Upon interaction of C3 with IgG.IC, C3b.C3b.IgG covalent complexes are formed that are detected on SDS-polyacrylamide gel electrophoresis by two bands corresponding to C3b.C3b (band A) and C3b.IgG (band B) covalent complexes. Sodium Dodecyl Sulfate 99-102 complement C3 Homo sapiens 40-43 11447230-2 2001 Upon interaction of C3 with IgG.IC, C3b.C3b.IgG covalent complexes are formed that are detected on SDS-polyacrylamide gel electrophoresis by two bands corresponding to C3b.C3b (band A) and C3b.IgG (band B) covalent complexes. Sodium Dodecyl Sulfate 99-102 complement C3 Homo sapiens 40-43 11447230-2 2001 Upon interaction of C3 with IgG.IC, C3b.C3b.IgG covalent complexes are formed that are detected on SDS-polyacrylamide gel electrophoresis by two bands corresponding to C3b.C3b (band A) and C3b.IgG (band B) covalent complexes. Sodium Dodecyl Sulfate 99-102 complement C3 Homo sapiens 40-43 10698338-6 1999 These complexes are detected on SDS-PAGE by two bands of molecular composition, C3alpha65-C3alpha43 (band A) and C3alpha65-heavy chain of the Ab (band B), which correspond to C3b-C3b and C3b-IgG covalent interaction respectively, and that identify opsonized IC (C3b-IC). Sodium Dodecyl Sulfate 32-35 complement C3 Homo sapiens 179-182 10698338-6 1999 These complexes are detected on SDS-PAGE by two bands of molecular composition, C3alpha65-C3alpha43 (band A) and C3alpha65-heavy chain of the Ab (band B), which correspond to C3b-C3b and C3b-IgG covalent interaction respectively, and that identify opsonized IC (C3b-IC). Sodium Dodecyl Sulfate 32-35 complement C3 Homo sapiens 179-182 10698338-6 1999 These complexes are detected on SDS-PAGE by two bands of molecular composition, C3alpha65-C3alpha43 (band A) and C3alpha65-heavy chain of the Ab (band B), which correspond to C3b-C3b and C3b-IgG covalent interaction respectively, and that identify opsonized IC (C3b-IC). Sodium Dodecyl Sulfate 32-35 complement C3 Homo sapiens 179-182 9580208-4 1998 C3 binding to IgG-IC generates IgG-C3b-C3b complexes which are detected by SDS-PAGE as two major bands: C3alpha65-heavy chain and C3alpha65-C3alpha43 covalent complexes. Sodium Dodecyl Sulfate 75-78 complement C3 Homo sapiens 35-38 9580208-4 1998 C3 binding to IgG-IC generates IgG-C3b-C3b complexes which are detected by SDS-PAGE as two major bands: C3alpha65-heavy chain and C3alpha65-C3alpha43 covalent complexes. Sodium Dodecyl Sulfate 75-78 complement C3 Homo sapiens 39-42 9368625-0 1997 Complement C3b fragment covalently linked to tetanus toxin increases lysosomal sodium dodecyl sulfate-stable HLA-DR dimer production. Sodium Dodecyl Sulfate 79-101 complement C3 Homo sapiens 11-14 9368625-3 1997 In the Epstein-Barr virus-transformed B cell line HOM 2, we detected a significant increase of sodium dodecyl sulfate (SDS)-stable major histocompatibility complex (MHC) class II molecules after exposure to C3b-TT as compared to unlinked C3b and TT. Sodium Dodecyl Sulfate 95-117 complement C3 Homo sapiens 207-210 9368625-3 1997 In the Epstein-Barr virus-transformed B cell line HOM 2, we detected a significant increase of sodium dodecyl sulfate (SDS)-stable major histocompatibility complex (MHC) class II molecules after exposure to C3b-TT as compared to unlinked C3b and TT. Sodium Dodecyl Sulfate 95-117 complement C3 Homo sapiens 238-241 9368625-3 1997 In the Epstein-Barr virus-transformed B cell line HOM 2, we detected a significant increase of sodium dodecyl sulfate (SDS)-stable major histocompatibility complex (MHC) class II molecules after exposure to C3b-TT as compared to unlinked C3b and TT. Sodium Dodecyl Sulfate 119-122 complement C3 Homo sapiens 207-210 9368625-3 1997 In the Epstein-Barr virus-transformed B cell line HOM 2, we detected a significant increase of sodium dodecyl sulfate (SDS)-stable major histocompatibility complex (MHC) class II molecules after exposure to C3b-TT as compared to unlinked C3b and TT. Sodium Dodecyl Sulfate 119-122 complement C3 Homo sapiens 238-241 9368625-5 1997 Similar results were obtained using HLA-DR1-transfected fibroblasts that do not express C3b complement receptors, indicating that the SDS-stable HLA-DR1 increase did not result simply from C3b opsonization but rather from a direct effect of C3b-TT linkage on peptide generation. Sodium Dodecyl Sulfate 134-137 complement C3 Homo sapiens 189-192 9368625-5 1997 Similar results were obtained using HLA-DR1-transfected fibroblasts that do not express C3b complement receptors, indicating that the SDS-stable HLA-DR1 increase did not result simply from C3b opsonization but rather from a direct effect of C3b-TT linkage on peptide generation. Sodium Dodecyl Sulfate 134-137 complement C3 Homo sapiens 189-192 9368625-6 1997 Exposure of HOM 2 cells to C3b-TT resulted in an increase in concentration of SDS-stable HLA-DR molecules in lysosomes but not in endosomes. Sodium Dodecyl Sulfate 78-81 complement C3 Homo sapiens 27-30 2428739-0 1986 SDS denaturation of complement factor C3 as a model for allosteric modifications occurring during C3b binding: demonstration of a profound conformational change by means of circular dichroism and quantitative immunoprecipitation. Sodium Dodecyl Sulfate 0-3 complement C3 Homo sapiens 98-101 7864806-3 1995 N-terminal analysis of the enzyme activity protein band, electroblotted from a SDS-acrylamide gel and with an assessed molecular mass of 19 kDa, showed an identical sequence to that of alpha-chain of human C3 complement component, suggesting the presence in this band of a complex formed by a complement C3-derived anaphylatoxin (C3a)-related fragment and the PLA2 linked side-by-side. Sodium Dodecyl Sulfate 79-82 complement C3 Homo sapiens 330-333 3257998-1 1988 A monoclonal antibody raised against SDS-denatured C3 was shown to react with both solid-phase C3a and unfragmented C3. Sodium Dodecyl Sulfate 37-40 complement C3 Homo sapiens 95-98 3384397-2 1988 This protein migrates Mr 45,000-70,000 dalton region with a broad singlet or doublet on SDS-PAGE, specifically binds to C3b and C4b, has an acidic pI around pH 4, is rich in proline in amino acid analysis, possesses both N-linked and O-linked oligosaccharides, generates iC3b by acting as a cofactor for I-mediated C3b cleavage, and does not disassemble the C3 convertases. Sodium Dodecyl Sulfate 88-91 complement C3 Homo sapiens 120-123 3384397-2 1988 This protein migrates Mr 45,000-70,000 dalton region with a broad singlet or doublet on SDS-PAGE, specifically binds to C3b and C4b, has an acidic pI around pH 4, is rich in proline in amino acid analysis, possesses both N-linked and O-linked oligosaccharides, generates iC3b by acting as a cofactor for I-mediated C3b cleavage, and does not disassemble the C3 convertases. Sodium Dodecyl Sulfate 88-91 complement C3 Homo sapiens 272-275 2443836-1 1987 Polyclonal antibodies raised in rabbits against sodium dodecyl sulphate (SDS)-denatured and reduced human complement factor C3 have in recent studies been shown to lack any reactivity towards native C3 but to react with antigens distinctly expressed by SDS-denatured C3 (C3(D) antigens). Sodium Dodecyl Sulfate 48-71 complement C3 Homo sapiens 271-285 2443836-1 1987 Polyclonal antibodies raised in rabbits against sodium dodecyl sulphate (SDS)-denatured and reduced human complement factor C3 have in recent studies been shown to lack any reactivity towards native C3 but to react with antigens distinctly expressed by SDS-denatured C3 (C3(D) antigens). Sodium Dodecyl Sulfate 73-76 complement C3 Homo sapiens 199-201 2443836-1 1987 Polyclonal antibodies raised in rabbits against sodium dodecyl sulphate (SDS)-denatured and reduced human complement factor C3 have in recent studies been shown to lack any reactivity towards native C3 but to react with antigens distinctly expressed by SDS-denatured C3 (C3(D) antigens). Sodium Dodecyl Sulfate 73-76 complement C3 Homo sapiens 271-285 2443836-1 1987 Polyclonal antibodies raised in rabbits against sodium dodecyl sulphate (SDS)-denatured and reduced human complement factor C3 have in recent studies been shown to lack any reactivity towards native C3 but to react with antigens distinctly expressed by SDS-denatured C3 (C3(D) antigens). Sodium Dodecyl Sulfate 253-256 complement C3 Homo sapiens 124-126 8387092-2 1993 This was confirmed by analysis of cell extracts by SDS-PAGE giving evidence for C3b-membrane protein complexes that were disrupted upon reduction. Sodium Dodecyl Sulfate 51-54 complement C3 Homo sapiens 80-83 1838328-6 1991 The C3 fragment, C3b, was confirmed to present on BAC1,4a,2a,3b particles by SDS-PAGE and immunoblot, and these particles were calculated to have approximately 25,000-30,000 C3b molecules per particle. Sodium Dodecyl Sulfate 77-80 complement C3 Homo sapiens 17-20 4047041-1 1985 The two common genetic variants of human C3, C3 S and C3 F, were purified and characterized by SDS-PAGE, agarose gel electrophoresis, isoelectric focusing and amino acid analysis. Sodium Dodecyl Sulfate 95-98 complement C3 Homo sapiens 41-58 3952470-4 1986 By using antihuman C3 antibodies, trypsin treatment, and sodium dodecyl sulphate washing, we were able to demonstrate C3b and iC3b on the agarose beads. Sodium Dodecyl Sulfate 57-80 complement C3 Homo sapiens 118-121 6642644-5 1983 Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of dithiothreitol and NH2OH eluates from the avidin-Sepharose showed that C3b bound to both heavy and light chains of the Ab. Sodium Dodecyl Sulfate 0-22 complement C3 Homo sapiens 132-135 6922882-3 1982 Analyses of iodipamide-treated NHS and purified C3 and factor B by reducing SDS-PAGE indicate that no macromolecular changes have occurred in C3 and factor B that can be ascribed to proteolysis (i.e., activation). Sodium Dodecyl Sulfate 76-79 complement C3 Homo sapiens 48-63 6339618-7 1983 protein corresponds to C3a by virtue of its co-migration in SDS polyacrylamide gels with purified C3a and with trypsin-generated C3a, by its detection in a radioimmunoassay for C3a, and by its contractile activity on the guinea pig ileum bioassay. Sodium Dodecyl Sulfate 60-63 complement C3 Homo sapiens 23-26 6218206-6 1983 Analysis by polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS-PAGE) of 125I-C3b in IC showed similar labeled peaks whether IC were pretreated with buffer or with I + H or were bound to RBC without pretreatment. Sodium Dodecyl Sulfate 50-72 complement C3 Homo sapiens 92-95 6218206-6 1983 Analysis by polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS-PAGE) of 125I-C3b in IC showed similar labeled peaks whether IC were pretreated with buffer or with I + H or were bound to RBC without pretreatment. Sodium Dodecyl Sulfate 74-77 complement C3 Homo sapiens 92-95 27210597-6 2016 The degradation of C3b into iC3b by factor I and factor H was enhanced by rTM as assessed by SDS-PAGE, confirming the previous observation. Sodium Dodecyl Sulfate 93-96 complement C3 Homo sapiens 19-22 7316962-3 1981 It was found that the C3b was probably covalently bound to the IgG in the aggregates, since C3b-IgG complexes could be demonstrated on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, after repeated washing with buffers containing high salt or boiling under denaturing conditions. Sodium Dodecyl Sulfate 135-158 complement C3 Homo sapiens 22-25 7316962-3 1981 It was found that the C3b was probably covalently bound to the IgG in the aggregates, since C3b-IgG complexes could be demonstrated on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, after repeated washing with buffers containing high salt or boiling under denaturing conditions. Sodium Dodecyl Sulfate 135-158 complement C3 Homo sapiens 92-95 32687811-3 2020 1.0M citric acid dissolved in 5% acetic acid (C3A) provides comparable results following both SDS-PAGE and two-dimensional gel electrophoresis, while also eliminating waste removal costs. Sodium Dodecyl Sulfate 94-97 complement C3 Homo sapiens 46-49 6156166-6 1980 C-3 was shown to undergo a specific, denaturation-dependent protein fragmentation in sodium dodecyl sulfate at 90 degrees C. The cleavage results in the partial conversion of the Mr = 135,000 subunit to fragments of Mr = 84,000 and 53,000. Sodium Dodecyl Sulfate 85-107 complement C3 Homo sapiens 0-3