PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26002640-2 2015 In the present study, a novel C1q domain containing protein from Crassostrea gigas (designated CgC1qDC-1) was isolated by liposaccharide-Sepharose 6B affinity chromatography. Sepharose 137-146 complement C1q A chain Homo sapiens 30-33 8172562-7 1993 The complex formation of C1q, the most basic serum protein, with this polyanion was demonstrated by several methods: agarose gel electrophoresis followed by immunoprecipitation in the gel and Coomassie staining; western blot analysis of C1q-PRP complexes; complex formation in electrophoretic separation of PRP; retardation of electrophoretic mobility of PRP was checked by blotting of this polysaccharide. Sepharose 117-124 complement C1q A chain Homo sapiens 25-28 8917617-4 1996 C1q (identified from its behaviour on SDS/PAGE, immunoreactivity with C1q-specific monoclonal antibodies and N-terminal sequencing data) was purified from serum by AMP-Sepharose chromatography. Sepharose 168-177 complement C1q A chain Homo sapiens 0-3 8917617-5 1996 The binding of C1q to AMP-Sepharose was inhibited by adenine nucleotides. Sepharose 26-35 complement C1q A chain Homo sapiens 15-18 7911495-4 1994 Covalent coupling of C1q to Sepharose beads allowed the affinity precipitation of a single 125-kDa band from surface iodinated PMN. Sepharose 28-37 complement C1q A chain Homo sapiens 21-24 8464426-3 1993 The availability of human and rat C1q allowed comparison of the two molecules, revealing differences in their mobility on SDS-PAGE as well as on agarose gel electrophoresis. Sepharose 145-152 complement C1q A chain Homo sapiens 34-37 2303724-2 1990 Complement protein C1q is coupled to Sepharose with an efficiency of 35%, giving 1.7 mg of C1q bound/ml of gel. Sepharose 37-46 complement C1q A chain Homo sapiens 19-22 1939090-4 1991 An affinity matrix of C1q tails coupled to Sepharose was used to select C1q-binding proteins from detergent extracts of surface-iodinated human monocytes, polymorphonuclear leukocytes, and the U937 cells. Sepharose 43-52 complement C1q A chain Homo sapiens 72-75 2303724-2 1990 Complement protein C1q is coupled to Sepharose with an efficiency of 35%, giving 1.7 mg of C1q bound/ml of gel. Sepharose 37-46 complement C1q A chain Homo sapiens 91-94 6975125-0 1981 Temperature-sensitive binding of solid phase C1q to aggregated human immunoglobulin G. The first component of complement (C1q) coupled to Sepharose by cyanogen bromide was found not to bind aggregated human gamma-globulin or immune complexes at room temperature, whereas at 4 degrees C binding was nearly complete. Sepharose 138-147 complement C1q A chain Homo sapiens 122-125 2820320-9 1987 Immune complexes in PMR and GCA differed from those previously characterized in rheumatoid arthritis (RA)1 purified by anti-C1q-Sepharose which contained immunoglobulins and C1q only. Sepharose 128-137 complement C1q A chain Homo sapiens 124-127 3485427-4 1986 Material specifically immunoabsorbed with Sepharose-anti-C1q antibody from a culture medium of cells that was metabolically labelled with [3H] proline or [35S] methionine demonstrated a polypeptide pattern identical with that of serum C1q on SDS/polyacrylamide-gel electrophoresis. Sepharose 42-51 complement C1q A chain Homo sapiens 57-60 3485427-4 1986 Material specifically immunoabsorbed with Sepharose-anti-C1q antibody from a culture medium of cells that was metabolically labelled with [3H] proline or [35S] methionine demonstrated a polypeptide pattern identical with that of serum C1q on SDS/polyacrylamide-gel electrophoresis. Sepharose 42-51 complement C1q A chain Homo sapiens 235-238 3872795-6 1985 C1q bound readily to native IgG-Sepharose but did not mediate the binding of Fn. Sepharose 32-41 complement C1q A chain Homo sapiens 0-3 6602941-4 1983 Fibronectin bound tightly to gelatin-Sepharose and C1q-Sepharose and this binding could be inhibited by gelatin but not by C1q. Sepharose 55-64 complement C1q A chain Homo sapiens 51-54 6976931-3 1981 The precipitation of C1q by the SO4(2-) groups in agarose gels was used as a means to rapidly monitor the elution of C1q. Sepharose 50-57 complement C1q A chain Homo sapiens 21-24 6976931-3 1981 The precipitation of C1q by the SO4(2-) groups in agarose gels was used as a means to rapidly monitor the elution of C1q. Sepharose 50-57 complement C1q A chain Homo sapiens 117-120 3183380-6 1988 SDS-PAGE of C1q-Sepharose eluates also revealed the presence of a 67,000 protein which was accompanied to varying degrees by a 94,000 constituent. Sepharose 16-25 complement C1q A chain Homo sapiens 12-15 3183380-7 1988 Because similar m.w., 125I-labeled proteins were recovered from C1q-Sepharose columns to which lysed, surface-labeled platelets had been applied, both 94,000 and 67,000 components appear to be platelet membrane constituents. Sepharose 68-77 complement C1q A chain Homo sapiens 64-67 3099175-3 1986 When purified 125I-C1q was incubated with SAP prior to Sepharose affinity chromatography, 125I-C1q was retained. Sepharose 55-64 complement C1q A chain Homo sapiens 19-22 3876986-2 1985 Affinity purified C1q was covalently coupled to a newly developed agarose polyacrolein microsphere beads immunoadsorbent. Sepharose 66-73 complement C1q A chain Homo sapiens 18-21 6606861-3 1983 Gel filtration chromatography (Sepharose 2B and 4B) of preincubated mixtures of C1q and Pl Fn yielded evidence of complex formation. Sepharose 31-40 complement C1q A chain Homo sapiens 80-83 6600764-2 1983 An assay for detection and quantitation of intra-cellular biosynthesis and secretion of C1q was then developed, using Sepharose beads covalently coated with goat monospecific anti-C1q IgG. Sepharose 118-127 complement C1q A chain Homo sapiens 88-91 6274149-1 1981 Under specified conditions purified C1q, activated C1r and C1s and C1r-C1s complexes were bound independently of Ca2+, to heparin-Sepharose, and could be eluted by an increasing salt gradient. Sepharose 130-139 complement C1q A chain Homo sapiens 36-39 119941-0 1979 Simultaneous determination of C1q and C3 levels in human serum by electroimmunodiffusion on agarose. Sepharose 92-99 complement C1q A chain Homo sapiens 30-33 6971771-3 1981 Inhibition assay of 125I-C1q binding to IgG-p-azobenzamidoethyl Sepharose 6B (IgG-Sepharose) by immune complexes was developed for the detection of circulating soluble immune complexes in the liver disease and was compared with polyclonal rheumatoid factor (pRF) binding inhibition assay and with C1q binding assay. Sepharose 64-73 complement C1q A chain Homo sapiens 25-28 6971771-3 1981 Inhibition assay of 125I-C1q binding to IgG-p-azobenzamidoethyl Sepharose 6B (IgG-Sepharose) by immune complexes was developed for the detection of circulating soluble immune complexes in the liver disease and was compared with polyclonal rheumatoid factor (pRF) binding inhibition assay and with C1q binding assay. Sepharose 64-73 complement C1q A chain Homo sapiens 297-300 7380940-0 1980 Simple method for the purification of C1q, a subcomponent of the first component of complement by affinity chromatography using IgG-Sepharose. Sepharose 132-141 complement C1q A chain Homo sapiens 38-41 773099-2 1976 Purified human C1q was covalently coupled to agarose or adsorbed to IgG-agarose resins. Sepharose 45-52 complement C1q A chain Homo sapiens 15-18 75238-12 1978 Second, C1s released by the activation can be quantitated by single radial diffusion if the agarose contains high concentrations of anti-C1q to confine C1, also containing C1s, to the area near the application well, and lesser concentrations of anti-C1s to permit free C1s to produce a measurable ring. Sepharose 92-99 complement C1q A chain Homo sapiens 137-140 773099-4 1976 Under conditions of antibody treatment which caused almost 100% inhibition of virus plaque formation, about 30% of formed 14C-labelled equine arteritis virus-antibody complexes was bound specifically to and desorbed from C1q-IgG agarose columns. Sepharose 229-236 complement C1q A chain Homo sapiens 221-224 773099-2 1976 Purified human C1q was covalently coupled to agarose or adsorbed to IgG-agarose resins. Sepharose 72-79 complement C1q A chain Homo sapiens 15-18 812922-2 1975 Moderately purified C1q is obtained by dialyzing fresh human serum in the presence of chelating agents at low ionic strength and then electrophoresing it in agarose. Sepharose 157-164 complement C1q A chain Homo sapiens 20-23 807640-3 1975 Affinity chromatography of serum-EDTA on Sepharose-IgG resulted in binding of only C1q and C1r. Sepharose 41-50 complement C1q A chain Homo sapiens 83-86 807640-5 1975 By the use of purified C1 proteins and Sepharose-IgG in binding studies it was confirmed that both C1q and C1r bind independently to sites on IgG and hold C1s and C1t by Ca++-dependent bonds. Sepharose 39-48 complement C1q A chain Homo sapiens 99-102 807640-9 1975 The evidence suggests that the spatial sequence of the components of the Sepharose-IgG-Serum C1 complex is: Sepharose-IgG: C1q: C1t: C1s: C1r: IgG-Sepharose. Sepharose 73-82 complement C1q A chain Homo sapiens 123-126 807640-9 1975 The evidence suggests that the spatial sequence of the components of the Sepharose-IgG-Serum C1 complex is: Sepharose-IgG: C1q: C1t: C1s: C1r: IgG-Sepharose. Sepharose 108-117 complement C1q A chain Homo sapiens 123-126 807640-9 1975 The evidence suggests that the spatial sequence of the components of the Sepharose-IgG-Serum C1 complex is: Sepharose-IgG: C1q: C1t: C1s: C1r: IgG-Sepharose. Sepharose 108-117 complement C1q A chain Homo sapiens 123-126 1168226-2 1975 Both sera contained material capable of precipitating C1q in agarose gel. Sepharose 61-68 complement C1q A chain Homo sapiens 54-57 4190971-0 1970 Reactions in agarose gel between C1q and aggregated gamma globulin. Sepharose 13-20 complement C1q A chain Homo sapiens 33-36