PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1292684-1 1992 The relationship between the concentration of serum amyloid protein (SAP) isolated from human serum and the parameters of the protein elution during gel-filtration and alos with the efficiency of Ca(2+)-dependent SAP binding with sepharose 4B was studied. Sepharose 230-239 amyloid P component, serum Homo sapiens 46-67 19660048-4 2009 SAP binds to some types of agarose in the presence of Ca(2+). Sepharose 27-34 amyloid P component, serum Homo sapiens 0-3 19660048-5 2009 We found that human SAP binds to an agarose with a K(D) of 7 x 10(-8) M and a B(max) of 2.1 microg SAP/mg wet weight agarose. Sepharose 36-43 amyloid P component, serum Homo sapiens 20-23 19660048-5 2009 We found that human SAP binds to an agarose with a K(D) of 7 x 10(-8) M and a B(max) of 2.1 microg SAP/mg wet weight agarose. Sepharose 36-43 amyloid P component, serum Homo sapiens 99-102 19660048-5 2009 We found that human SAP binds to an agarose with a K(D) of 7 x 10(-8) M and a B(max) of 2.1 microg SAP/mg wet weight agarose. Sepharose 117-124 amyloid P component, serum Homo sapiens 20-23 19660048-5 2009 We found that human SAP binds to an agarose with a K(D) of 7 x 10(-8) M and a B(max) of 2.1 microg SAP/mg wet weight agarose. Sepharose 117-124 amyloid P component, serum Homo sapiens 99-102 19660048-6 2009 Mixing this agarose 1 : 5 w/v with 30 microg/mL human SAP (the average SAP concentration in normal serum) in a buffer containing 2 mM Ca(2+) reduced the free SAP concentration to approximately 0.02 microg/mL, well below the concentration that inhibits fibrocyte differentiation. Sepharose 12-19 amyloid P component, serum Homo sapiens 54-57 19660048-6 2009 Mixing this agarose 1 : 5 w/v with 30 microg/mL human SAP (the average SAP concentration in normal serum) in a buffer containing 2 mM Ca(2+) reduced the free SAP concentration to approximately 0.02 microg/mL, well below the concentration that inhibits fibrocyte differentiation. Sepharose 12-19 amyloid P component, serum Homo sapiens 71-74 19660048-6 2009 Mixing this agarose 1 : 5 w/v with 30 microg/mL human SAP (the average SAP concentration in normal serum) in a buffer containing 2 mM Ca(2+) reduced the free SAP concentration to approximately 0.02 microg/mL, well below the concentration that inhibits fibrocyte differentiation. Sepharose 12-19 amyloid P component, serum Homo sapiens 71-74 7592941-6 1995 SAP-Sepharose specifically bound the 160-kDa fragment, suggesting that the central core of C4BP contains the binding site for SAP. Sepharose 4-13 amyloid P component, serum Homo sapiens 0-3 7592941-6 1995 SAP-Sepharose specifically bound the 160-kDa fragment, suggesting that the central core of C4BP contains the binding site for SAP. Sepharose 4-13 amyloid P component, serum Homo sapiens 126-129 15478465-4 2004 SAP was purified from serum by affinity chromatography using phosphorylethanolamine-coupled ECH-sepharose 4B. Sepharose 96-108 amyloid P component, serum Homo sapiens 0-3 1292684-1 1992 The relationship between the concentration of serum amyloid protein (SAP) isolated from human serum and the parameters of the protein elution during gel-filtration and alos with the efficiency of Ca(2+)-dependent SAP binding with sepharose 4B was studied. Sepharose 230-239 amyloid P component, serum Homo sapiens 69-72 1292684-1 1992 The relationship between the concentration of serum amyloid protein (SAP) isolated from human serum and the parameters of the protein elution during gel-filtration and alos with the efficiency of Ca(2+)-dependent SAP binding with sepharose 4B was studied. Sepharose 230-239 amyloid P component, serum Homo sapiens 213-216 3211159-2 1988 In the presence of calcium, SAP binds to certain complex polysaccharides, including agarose and zymosan. Sepharose 84-91 amyloid P component, serum Homo sapiens 28-31 1377216-5 1992 We found evidence for the formation of a high-affinity 1:1 complex between SAP and heparin and for inhibition of binding of both thrombin and antithrombin III to heparin-Sepharose by SAP. Sepharose 170-179 amyloid P component, serum Homo sapiens 75-78 1377216-5 1992 We found evidence for the formation of a high-affinity 1:1 complex between SAP and heparin and for inhibition of binding of both thrombin and antithrombin III to heparin-Sepharose by SAP. Sepharose 170-179 amyloid P component, serum Homo sapiens 183-186 2138034-5 1990 Removal of sialic acids from SAP reduced the calcium-dependent binding activity for agarose by 7%, suggesting the terminal sialic acids were partially responsible for the binding. Sepharose 84-91 amyloid P component, serum Homo sapiens 29-32 3211159-3 1988 While the binding of SAP to agarose involves interaction with a galactose pyruvate acetal, the ligand in zymosan has not been defined. Sepharose 28-35 amyloid P component, serum Homo sapiens 21-24 3105045-5 1987 SAP bound to TNP-agarose was eluated by either EDTA or p-nitrophenylarsonic acid. Sepharose 17-24 amyloid P component, serum Homo sapiens 0-3 3276308-3 1988 A specific binding of SAP to hyaluronic acid, heparan sulfate, and dermatan sulfate was also confirmed by the fact that these glycosaminoglycans blocked the binding of SAP to agarose, a specific ligand of SAP. Sepharose 175-182 amyloid P component, serum Homo sapiens 22-25 3276308-3 1988 A specific binding of SAP to hyaluronic acid, heparan sulfate, and dermatan sulfate was also confirmed by the fact that these glycosaminoglycans blocked the binding of SAP to agarose, a specific ligand of SAP. Sepharose 175-182 amyloid P component, serum Homo sapiens 168-171 3276308-3 1988 A specific binding of SAP to hyaluronic acid, heparan sulfate, and dermatan sulfate was also confirmed by the fact that these glycosaminoglycans blocked the binding of SAP to agarose, a specific ligand of SAP. Sepharose 175-182 amyloid P component, serum Homo sapiens 168-171 2948956-2 1987 The binding of human SAP to heparan sulfate and dermatan sulfate was studied using Sepharose-immobilized SAP. Sepharose 83-92 amyloid P component, serum Homo sapiens 21-24 2948956-2 1987 The binding of human SAP to heparan sulfate and dermatan sulfate was studied using Sepharose-immobilized SAP. Sepharose 83-92 amyloid P component, serum Homo sapiens 105-108 3192306-3 1988 We present evidence suggestive of varying affinities of SAP for agarose, to which SAP is known to adsorb in the presence of calcium, by fused rocket immunoelectrophoresis. Sepharose 64-71 amyloid P component, serum Homo sapiens 56-59 3192306-3 1988 We present evidence suggestive of varying affinities of SAP for agarose, to which SAP is known to adsorb in the presence of calcium, by fused rocket immunoelectrophoresis. Sepharose 64-71 amyloid P component, serum Homo sapiens 82-85 6707579-3 1984 Although the binding to agarose, a linear galactan hydrocolloid derived from some marine algae, is unlikely per se to be related to the physiological function of SAP, it does provide a model system in which to explore the precise ligand requirements of SAP. Sepharose 24-31 amyloid P component, serum Homo sapiens 253-256 3099175-2 1986 It is known that SAP binds Sepharose in the presence of calcium. Sepharose 27-36 amyloid P component, serum Homo sapiens 17-20 3722822-8 1986 Chromatography of serum on TNP-Sepharose provided a efficient and simple way of purifying SAP. Sepharose 31-40 amyloid P component, serum Homo sapiens 90-93 6707579-4 1984 We report here that the amount of SAP from human, mouse, and plaice (Pleuronectes platessa L.) serum able to bind to agarose from different sources reflect precisely their pyruvate content. Sepharose 117-124 amyloid P component, serum Homo sapiens 34-37 6707579-5 1984 Methylation with diazomethane of the carboxyl groups in the pyruvate moiety of agarose completely abolishes SAP binding to agarose. Sepharose 79-86 amyloid P component, serum Homo sapiens 108-111 6707579-5 1984 Methylation with diazomethane of the carboxyl groups in the pyruvate moiety of agarose completely abolishes SAP binding to agarose. Sepharose 123-130 amyloid P component, serum Homo sapiens 108-111 6807178-7 1982 While the identity of natural ligand for SAP is as yet unknown, it is likely to resemble the glycosidic subunits in agarose. Sepharose 116-123 amyloid P component, serum Homo sapiens 41-44 6807178-5 1982 Precipitation of purified SAP by calcium could be prevented by pretreatment with acid hydrolysates of agarose or SP Sephadex, matrices for which SAP has a calcium-dependent affinity. Sepharose 102-109 amyloid P component, serum Homo sapiens 26-29 6807178-5 1982 Precipitation of purified SAP by calcium could be prevented by pretreatment with acid hydrolysates of agarose or SP Sephadex, matrices for which SAP has a calcium-dependent affinity. Sepharose 102-109 amyloid P component, serum Homo sapiens 145-148 7086148-3 1982 It was then gel filtered on Ultrogel AcA44 (acrylamide-agarose beads) in the presence of calcium ions, combining molecular sieve chromatography with removal of contaminating SAP by its affinity of agarose. Sepharose 197-204 amyloid P component, serum Homo sapiens 174-177 7086148-6 1982 SAP was isolated from normal serum by calcium-dependent affinity chromatography on unsubstituted Sepharose beads, followed by solid-phase immunoabsorption of contaminants and finally gel filtration on Sephacryl S-300. Sepharose 97-106 amyloid P component, serum Homo sapiens 0-3 6793685-5 1981 SAP, which had been aggregated either by direct conjugation to CNBr-activated Sepharose beads, or by complexing with anti-SAP antibodies immobilized on such beads, selectively took up fibronectin and C4-binding protein from whole normal human serum. Sepharose 78-87 amyloid P component, serum Homo sapiens 0-3 6793685-7 1981 Experiments with isolated fibronectin and SAP complexed by anti-SAP-Sepharose indicated that close association of pairs of SAP molecules was required for fibronectin to be bound and that each SAP dimer was capable of taking up a single molecule of fibronectin. Sepharose 68-77 amyloid P component, serum Homo sapiens 42-45 6793685-7 1981 Experiments with isolated fibronectin and SAP complexed by anti-SAP-Sepharose indicated that close association of pairs of SAP molecules was required for fibronectin to be bound and that each SAP dimer was capable of taking up a single molecule of fibronectin. Sepharose 68-77 amyloid P component, serum Homo sapiens 64-67 6793685-7 1981 Experiments with isolated fibronectin and SAP complexed by anti-SAP-Sepharose indicated that close association of pairs of SAP molecules was required for fibronectin to be bound and that each SAP dimer was capable of taking up a single molecule of fibronectin. Sepharose 68-77 amyloid P component, serum Homo sapiens 64-67 6793685-7 1981 Experiments with isolated fibronectin and SAP complexed by anti-SAP-Sepharose indicated that close association of pairs of SAP molecules was required for fibronectin to be bound and that each SAP dimer was capable of taking up a single molecule of fibronectin. Sepharose 68-77 amyloid P component, serum Homo sapiens 64-67