PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2140680-1 1990 Modifications to the commonly employed lysine Sepharose affinity chromatography method for the purification of plasminogen from human plasma, give a preparation of native, Glu-plasminogen which is free of plasmin contamination. Sepharose 46-55 plasminogen Homo sapiens 111-118 2140680-0 1990 Modifications to the lysine Sepharose method of plasminogen purification which ensure plasmin-free Glu-plasminogen. Sepharose 28-37 plasminogen Homo sapiens 48-55 2534245-4 1989 These unbound to plasmin-Sepharose fibronectin fragments were found to stimulate proliferation of human embryonal fibroblasts in cell culture, whereas the plasmin-Sepharose bound peptides did not exhibit any effects on proliferation. Sepharose 163-172 plasminogen Homo sapiens 155-162 2534245-1 1989 Plasmin, immobilized on Sepharose, was used for isolation of human blood plasma fibronectin fragments obtained after proteolysis. Sepharose 24-33 plasminogen Homo sapiens 0-7 2534245-2 1989 Under definite conditions the major part of the fibronectin fragments, liberated during proteolysis, remained to be bound to plasmin-Sepharose. Sepharose 133-142 plasminogen Homo sapiens 125-132 2534245-3 1989 As shown by electrophoretic analysis, the fraction of fragments bound to plasmin-Sepharose constituted mainly "heavy" (greater than or equal to 120 kD) peptides and one "light" (29 kD) peptide, while only "light" fragments (less than or equal to 45 kD) were detected in the free unbound fraction. Sepharose 81-90 plasminogen Homo sapiens 73-80 2534245-4 1989 These unbound to plasmin-Sepharose fibronectin fragments were found to stimulate proliferation of human embryonal fibroblasts in cell culture, whereas the plasmin-Sepharose bound peptides did not exhibit any effects on proliferation. Sepharose 25-34 plasminogen Homo sapiens 17-24 2522013-6 1989 Limited elastase proteolysis of plasminogen and plasmin resulted in the generation of two distinct thrombospondin binding domains, one of which was retained on lysine-agarose. Sepharose 167-174 plasminogen Homo sapiens 32-39 2432967-4 1987 The appearance of proteins lacking biological specificity to lysin-sepharose in the plasminogen preparation shows the ability of activated plasminogen and plasmin to form complexes with these proteins and demonstrates the retention of the functional activity in lysin-binding regions on their molecules. Sepharose 67-76 plasminogen Homo sapiens 84-91 2942536-3 1986 Using an enzyme-linked immunosorbent assay and a TSP-Sepharose affinity bead-binding assay we have found that Plg-TSP complex formation was markedly enhanced (up to 5-fold) when catalytic concentrations of Plg activators were included in the reaction mixtures. Sepharose 53-62 plasminogen Homo sapiens 110-113 2942536-3 1986 Using an enzyme-linked immunosorbent assay and a TSP-Sepharose affinity bead-binding assay we have found that Plg-TSP complex formation was markedly enhanced (up to 5-fold) when catalytic concentrations of Plg activators were included in the reaction mixtures. Sepharose 53-62 plasminogen Homo sapiens 206-209 2943315-7 1986 Also, stimulation of plasmin formation is not observed with dextran sulfate or chondroitin sulfate A, B, or C. Analyses of heparin fractions after separation on columns of antithrombin III-Sepharose suggest that both the high-affinity and the low-affinity fractions, which have dramatically different anticoagulant activity, have similar activity toward the fibrinolytic components. Sepharose 189-198 plasminogen Homo sapiens 21-28 3161540-0 1985 Quantitative characterization of the binding of plasminogen to intact fibrin clots, lysine-sepharose, and fibrin cleaved by plasmin. Sepharose 91-100 plasminogen Homo sapiens 48-55 3721516-1 1986 Phenotyping of plasma plasminogen (PLG) was carried out by the method of agarose gel isoelectric focusing followed by immunofixation or immunoblotting. Sepharose 73-80 plasminogen Homo sapiens 22-33 3721516-1 1986 Phenotyping of plasma plasminogen (PLG) was carried out by the method of agarose gel isoelectric focusing followed by immunofixation or immunoblotting. Sepharose 73-80 plasminogen Homo sapiens 35-38 3160727-4 1985 In the present study, the digestion of vWF multimers by plasmin was analyzed by sodium dodecyl sulfate-agarose gel electrophoresis and radioimmunoblotting. Sepharose 103-110 plasminogen Homo sapiens 56-63 2931900-1 1985 Plasmin, free of an activator, was obtained after activation of the highly purified human plasminogen by means of trypsin immobilized on Sepharose 4B and after removal of the enzyme from the system. Sepharose 137-149 plasminogen Homo sapiens 0-7 2944852-1 1986 The light chain of plasmin, prepared by selective reduction of the interchain disulfide bridges, can be separated from the heavy chain by affinity adsorption onto Kunitz inhibitor/Sepharose. Sepharose 180-189 plasminogen Homo sapiens 19-26 3088754-6 1986 The extent of binding of the two pro-urokinases and their plasmin-activated forms to fibrin-sepharose decreased in the following order: 55 kd pro-urokinase 30 kd pro-urokinase 55 kd urokinase 30 kd urokinase. Sepharose 92-101 plasminogen Homo sapiens 58-65 4008652-7 1985 Rocket immunoelectrophoresis of mixtures of the purified radiolabeled proteins into anti-Plg containing agarose also confirmed trimolecular complex formation. Sepharose 104-111 plasminogen Homo sapiens 89-92 4008652-6 1985 HRGP covalently cross-linked to Sepharose 4B simultaneously bound both 125I-TSP and 131I-Plg, confirming trimolecular complex formation. Sepharose 32-44 plasminogen Homo sapiens 89-92 3161540-5 1985 Limited digestion of fibrin by plasmin created additional binding sites for plasminogen with Kd values similar to the binding of plasminogen to lysine-Sepharose. Sepharose 151-160 plasminogen Homo sapiens 31-38 154322-1 1978 The primary inhibitor of plasmin in human plasma was purified by a four-step procedure involving fractional (NH(4))(2)SO(4) precipitation, ion-exchange chromatography on a column of DEAE-Sepharose CL-6B and affinity chromatography on both a plasminogen-CH-Sepharose 4B column and a column of 6-aminohexanoic acid covalently coupled through the carboxylate function to AH-Sepharose 4B. Sepharose 187-196 plasminogen Homo sapiens 25-32 3834881-1 1985 Distribution of PLG types was studied in a sample of the Polish population numbering 230 subjects by the method of high-voltage agarose electrophoresis. Sepharose 128-135 plasminogen Homo sapiens 16-19 7095815-1 1982 Three new phenotypes of plasminogen system, named PLG 3-1, PLG 1-M and PLG 1-C, were found in sera from healthy Japanese persons by the agarose gel isoelectric focusing followed by the methods of immunofixation and caseinolysis. Sepharose 136-143 plasminogen Homo sapiens 50-53 6449829-3 1980 This substance, designated "plasmin", was separated from plasmin and kallikrein in a three-step procedure using columns of lysine-Sepharose, DEAE-Sephadex A-50, and arginine-Sepharose. Sepharose 130-139 plasminogen Homo sapiens 28-35 6449829-3 1980 This substance, designated "plasmin", was separated from plasmin and kallikrein in a three-step procedure using columns of lysine-Sepharose, DEAE-Sephadex A-50, and arginine-Sepharose. Sepharose 174-183 plasminogen Homo sapiens 28-35 2422420-3 1985 alpha 2-Macroglobulin-plasmin complexes were purified from urokinase-activated plasma by affinity chromatography on lysine-Sepharose and gel filtration on Ultrogel AcA 22. Sepharose 123-132 plasminogen Homo sapiens 22-29 6447502-2 1980 An inhibitor of the plasma proteinase plasmin (EC 3.4.21.7) was partially purified from washed and lysed human blood platelets by (NH4)2SO4 fractionation and affinity chromatrography on Sepharose-linked purified plasminogen. Sepharose 186-195 plasminogen Homo sapiens 38-45 6447502-8 1980 The inhibitor increased the mobility in agarose-gel electrophoresis of purified activator-free plasmin or 125I-labelled plasmin, as demonstrated by crossed-immunoelectrophoresis against specific immunoglobulins against plasminogen or by radioautography. Sepharose 40-47 plasminogen Homo sapiens 95-102 6447502-8 1980 The inhibitor increased the mobility in agarose-gel electrophoresis of purified activator-free plasmin or 125I-labelled plasmin, as demonstrated by crossed-immunoelectrophoresis against specific immunoglobulins against plasminogen or by radioautography. Sepharose 40-47 plasminogen Homo sapiens 120-127 157580-3 1979 The plasminogen immobilized on bromocyanogen-activated sepharose and cellulose, like soluble proenzyme, has no activity of plasmin and retains the ability of being activated with streptokinase in catalytic amounts. Sepharose 55-64 plasminogen Homo sapiens 4-11 154322-1 1978 The primary inhibitor of plasmin in human plasma was purified by a four-step procedure involving fractional (NH(4))(2)SO(4) precipitation, ion-exchange chromatography on a column of DEAE-Sepharose CL-6B and affinity chromatography on both a plasminogen-CH-Sepharose 4B column and a column of 6-aminohexanoic acid covalently coupled through the carboxylate function to AH-Sepharose 4B. Sepharose 256-265 plasminogen Homo sapiens 25-32 177230-1 1976 Complex formation in vitro between human alpha2-macroglobulin and the human proteases cationic trypsin, chymotrypsin, plasmin and granulocyte elastase and collagenase was clearly visualized by the use of thin-layer electrofocusing in polyacrylamide gel followed by electrophoresis in agarose gel containing antibodies against human alpha2-macroglobulin. Sepharose 284-291 plasminogen Homo sapiens 118-125 142314-0 1977 The inactivation of thrombin and plasmin by antithrombin III in the presence of sepharose-heparin. Sepharose 80-89 plasminogen Homo sapiens 33-40 134997-1 1976 A functionally active human plasmin light (B) chain derivative, stabilized by the streptomyces plasmin inhibitor leupeptin, was isolated from a partially reduced and alkylated enzyme preparation by an affinity chromatography method with a L-lysine-substituted Sepharose column. Sepharose 260-269 plasminogen Homo sapiens 28-35 125463-6 1975 in the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5-1.6 moles tranexamic acid per one mole protein. Sepharose 159-168 plasminogen Homo sapiens 48-55 16336793-0 2005 A method for direct application of human plasmin on a dithiothreitol-containing agarose stacking gel system. Sepharose 80-87 plasminogen Homo sapiens 41-48 16444438-6 2006 In particular, a co-amplified gene on chromosome 2 mimicking a 14 bp deletion in exon 5 of the plasminogen gene was identified by sequencing two different bands obtained from a long run of the PCR exon 5 product in NuSieve agarose gel, and by PstI restriction enzyme analysis of the same amplicons. Sepharose 223-230 plasminogen Homo sapiens 95-106 4244455-5 1970 Agarose and acrylamide gel immunoelectrophoresis of a plasmin, inhibitor mixture showed the appearance of an additional precipitin band with immunologic reactivity similar to that of the untreated inhibitor. Sepharose 0-7 plasminogen Homo sapiens 54-61 18766256-3 2008 Following protein refolding and purification on lysine-Sepharose, the conversion of the recombinant molecule Delta(K2-K5)Pg to the active enzyme mutant Delta(K2-K5)Pm by plasminogen activators was evaluated, and functional characteristics of the simplified plasmin were studied. Sepharose 55-64 plasminogen Homo sapiens 170-177 16336793-1 2005 A new simplified procedure for identifying human plasmin was developed using a DTT copolymerized agarose stacking gel (ASG) system. Sepharose 97-104 plasminogen Homo sapiens 49-56 8672509-6 1996 Preliminary, we screened Lib#1 against human plasmin (PLA, EC 3.4.21.7) immobolized on agarose to enrich for phage displaying variants with PLA affinity. Sepharose 87-94 plasminogen Homo sapiens 45-52 8672509-6 1996 Preliminary, we screened Lib#1 against human plasmin (PLA, EC 3.4.21.7) immobolized on agarose to enrich for phage displaying variants with PLA affinity. Sepharose 87-94 plasminogen Homo sapiens 54-57 8672509-8 1996 Lib#2 (allowing approximately 50 million amino-acid sequences) was screened against PLA-agarose to isolate highest affinity binders. Sepharose 88-95 plasminogen Homo sapiens 84-87 7683664-6 1993 When mixtures of plasmin and STAR were adsorbed to lysine-Sepharose, STAR adsorbed quantitatively (96 +/- 1%) to the gel, whereas it was nearly quantitatively recovered in the unbound fraction (92 +/- 4%) after addition of alpha 2-antiplasmin to the mixture. Sepharose 58-67 plasminogen Homo sapiens 17-24 7683664-7 1993 Scatchard analysis of the binding of STAR to plasmin-Sepharose yielded a dissociation constant of 55 nM, whereas no specific binding of STAR to plasmin-alpha 2-antiplasmin-Sepharose could be demonstrated. Sepharose 53-62 plasminogen Homo sapiens 45-52 1657983-10 1991 Biosynthetically labeled 40-kDa protein coprecipitated with t-PA- or Lys-PLG-Sepharose beads, but not with unconjugated Sepharose. Sepharose 77-86 plasminogen Homo sapiens 73-76 8198542-6 1994 Oleic acid at 200 microM also effectively displaced plasmin prebound to a polylysine-Sepharose column. Sepharose 85-94 plasminogen Homo sapiens 52-59 1533307-4 1992 The acylated and non-acylated plasminogen and plasmin were coupled to cyanogen bromide-activated Sepharose 4B and evaluated for streptokinase purification. Sepharose 97-109 plasminogen Homo sapiens 30-37