PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10217155-1 1999 The separation of complement factors C3 and C3b by isotachophoresis in 1% agarose gel followed by immunoprecipitation and quantification is presented. Sepharose 74-81 complement C3 Homo sapiens 44-47 11402501-11 2001 Furthermore, fH and factor I (fI)-mediated cleavage of agarose bound C3b into iC3b was decreased in the presence of pepAred. Sepharose 55-62 complement C3 Homo sapiens 69-72 2948272-0 1986 Phagocytosis of agarose beads by receptors for C3b (CR1) and iC3b (CR3) on human alveolar macrophages cultured on fibronectin in vitro. Sepharose 16-23 complement C3 Homo sapiens 47-50 8125130-8 1994 The latter was also immunoprecipitated with anti-Fc-Sepharose from the pepsin digestion supernatants of 14C-labeled-C3b-IgG complexes. Sepharose 52-61 complement C3 Homo sapiens 116-119 1639919-1 1992 Aminophenylboronate-substituted agarose in 20 mM N-2-hydroxyethylpiperazine-N"-2-ethanesulphonic acid, pH 8.5, selectively adsorbs immunoglobulins and complement factors C3 and C4 from human serum. Sepharose 32-39 complement C3 Homo sapiens 170-179 1835839-1 1991 Various amounts of the activation fragment C3b of the complement (C) protein C3 were coupled to Sepharose 4B by catalysis with the C3 convertase of the alternative pathway of C. The binding of radioactively labelled C proteins B and H (= factor H) to the C3b-carrying particles was assayed. Sepharose 96-105 complement C3 Homo sapiens 43-46 2037387-6 1991 The most common biological effects of PP over protein-A sepharose were significant drops in IgG (66% of pre-PP values), CH50 and C3 (73% of pre-PP values) and a significant generation of C3a and C5a anaphylatoxins. Sepharose 56-65 complement C3 Homo sapiens 187-190 2136879-1 1990 Soluble polymerized human C3b and C3b bound to Sepharose induced the production of cell-associated IL-1 and the extracellular release of IL-1 activity from cultured human adherent monocytes. Sepharose 47-56 complement C3 Homo sapiens 26-29 2136879-1 1990 Soluble polymerized human C3b and C3b bound to Sepharose induced the production of cell-associated IL-1 and the extracellular release of IL-1 activity from cultured human adherent monocytes. Sepharose 47-56 complement C3 Homo sapiens 34-37 2953614-8 1987 C3b purified by anion-exchange fast protein liquid chromatography on a Mono Q column or eluted from a monoclonal anti-C3b-Sepharose retained its modulating activity, while native C3 or C3 fragments such as iC3b, C3c or C3d,g were ineffective. Sepharose 122-131 complement C3 Homo sapiens 0-3 2953614-8 1987 C3b purified by anion-exchange fast protein liquid chromatography on a Mono Q column or eluted from a monoclonal anti-C3b-Sepharose retained its modulating activity, while native C3 or C3 fragments such as iC3b, C3c or C3d,g were ineffective. Sepharose 122-131 complement C3 Homo sapiens 118-121 2148644-0 1990 Phagocytosis of agarose beads by receptors for C3b (CR1) and iC3b (CR3) on alveolar macrophages from patients with sarcoidosis. Sepharose 16-23 complement C3 Homo sapiens 47-50 6139373-10 1983 A tryptic peptide containing the 3H label was isolated following digestion of [3H]C3b on activated thiol-Sepharose. Sepharose 105-114 complement C3 Homo sapiens 82-85 3905970-3 1985 By this method we have demonstrated the existence of multiple molecular forms of the complement factors C3 and factor B in serum from 2 species, man and chicken, after electrophoretic separation in agarose. Sepharose 198-205 complement C3 Homo sapiens 104-119 6699545-4 1984 The activation of zymosan was C3 dependent, and C3b-coated Sepharose was also an effective stimulant. Sepharose 59-68 complement C3 Homo sapiens 48-51 6642644-3 1983 Ab molecules were then eluted from Pn, and C3b-associated molecules were purified on avidin-Sepharose. Sepharose 92-101 complement C3 Homo sapiens 43-46 3488995-7 1986 When C3 was cleaved with trypsin, C3b and C3d but not C3c bound to laminin-Sepharose. Sepharose 75-84 complement C3 Homo sapiens 34-37 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. Sepharose 138-145 complement C3 Homo sapiens 118-121 3952470-6 1986 We conclude that in vitro human monocytes produce and secrete the essential factors for activation and propagation of the alternative complement pathway (factors C3, B, D, H and I), which becomes evident with an external activator like agarose beads in the cultures. Sepharose 236-243 complement C3 Homo sapiens 162-179 3952470-7 1986 The activation of complement by agarose beads results in the attachment of C3b and iC3b to the surface of the beads, which are then phagocytosed by means of C3b and iC3b receptors on the monocytes. Sepharose 32-39 complement C3 Homo sapiens 75-78 3952470-7 1986 The activation of complement by agarose beads results in the attachment of C3b and iC3b to the surface of the beads, which are then phagocytosed by means of C3b and iC3b receptors on the monocytes. Sepharose 32-39 complement C3 Homo sapiens 84-87 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. Sepharose 105-112 complement C3 Homo sapiens 41-58 6379853-6 1984 Since agarose beads are activators of the alternative pathway of complement, and fibronectin is reported to bind to factor C3, we speculate that cell-derived C3b is bound to the beads and fibronectin-coated beads are ingested by the phagocytes via complement C3b receptors on the cells. Sepharose 6-13 complement C3 Homo sapiens 158-161 6544185-2 1984 This partially denatured C3 (C3i) was coupled to activated Thiol-Sepharose via its single SH group. Sepharose 65-74 complement C3 Homo sapiens 25-27 6544185-2 1984 This partially denatured C3 (C3i) was coupled to activated Thiol-Sepharose via its single SH group. Sepharose 65-74 complement C3 Homo sapiens 29-32 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. Sepharose 110-119 complement C3 Homo sapiens 132-135 7150233-0 1982 A general method for affinity purification of complement component C3b using factor H-sepharose. Sepharose 86-95 complement C3 Homo sapiens 67-70 6222469-2 1983 By using isolated human complement factors C3, B and D, agarose beads were coated with C3b. Sepharose 56-63 complement C3 Homo sapiens 43-54 6222469-2 1983 By using isolated human complement factors C3, B and D, agarose beads were coated with C3b. Sepharose 56-63 complement C3 Homo sapiens 87-90 6222469-4 1983 Agarose beads coated with C3b or C3bi bound strongly to monocytes. Sepharose 0-7 complement C3 Homo sapiens 26-29 7150233-1 1982 Complement component C3b has been purified from human, rabbit and bovine serum by affinity chromatography on human factor H-Sepharose after preliminary fractionation by poly(ethylene glycol) and DEAE-Sepharose. Sepharose 124-133 complement C3 Homo sapiens 0-24 7150233-3 1982 Binding of C3b to factor H-Sepharose is equimolar, has a sharp optimum pH at 7.6 and is quite sensitive to ionic strength. Sepharose 27-36 complement C3 Homo sapiens 11-14 114594-2 1979 A simple electrophoretic technique employing commercially available agarose films is described for the routine estimation of plasma complement C3 conversion. Sepharose 68-75 complement C3 Homo sapiens 132-145 6785350-2 1981 When whole serum containing [125I] C3 was incubated with agarose-thioglucose, labeled C3b was taken up in a form that was not removed by 2 M NaCl but was released by 10 mM dithiothreitol. Sepharose 57-64 complement C3 Homo sapiens 86-89 7305916-3 1981 Binding of C3 to Sepharose-trypsin is saturable, with a maximum of 25-26 molecules of C3b bound per molecule of trypsin. Sepharose 17-26 complement C3 Homo sapiens 86-89 6776155-2 1980 We describe a method utilising immunofixation after agarose or cellulose acetate membrane electrophoresis which allows large batches of samples to be screened rapidly for the presence of activation products of C3 and factor B. Sepharose 52-59 complement C3 Homo sapiens 210-225 7050289-5 1982 The capacity of C3a(70-77)-Sepharose,m but not Sepharose alone, to adsorb or inactivate mononuclear leukocytes required for the generation of LIF activity established a direct interaction. Sepharose 27-36 complement C3 Homo sapiens 16-19 7050289-6 1982 Analysis of the lymphocytes in the effluent from C3a(70-77)-Sepharose columns, using monoclonal antibodies to surface antigens, showed a selective depletion of the helper/inducer population of lymphocytes. Sepharose 60-69 complement C3 Homo sapiens 49-52 6912277-11 1981 Organomercurial agarose was employed for the rapid removal of sulfhydryl-bearing, hemolytically inactive forms of C3 and C3b from native hemolytically active C3. Sepharose 16-23 complement C3 Homo sapiens 121-124 126576-9 1975 C3 was activated and the resulting C3b fragment fixed on agarose by incubating C3 with trypsin covalently bound to the agarose. Sepharose 57-64 complement C3 Homo sapiens 35-38 126576-9 1975 C3 was activated and the resulting C3b fragment fixed on agarose by incubating C3 with trypsin covalently bound to the agarose. Sepharose 119-126 complement C3 Homo sapiens 35-38 126576-10 1975 The agarose-C3b intermediate was capable of binding GBG provided Mg++ was present. Sepharose 4-11 complement C3 Homo sapiens 12-15 28757372-1 2017 Two novel magnetic agarose bead based assays have been developed to measure complement component C5 interaction with C3b and the Factor I Modules (FIMs) of C7. Sepharose 19-26 complement C3 Homo sapiens 117-120 28757372-2 2017 One innovation was to couple C3b onto the magnetic agarose bead using the alternative pathway C3 convertase, which resulted in a linkage of the ligand by a covalent ester bond. Sepharose 51-58 complement C3 Homo sapiens 29-32 21683785-7 2011 On agarose gel electrophoresis, C3a comigrated with MDA-LDL and MAA-LDL, but not with native LDL or CuOx-LDL. Sepharose 3-10 complement C3 Homo sapiens 32-35