PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17938226-8 2007 Our observation that Plg blocked the binding of anti-alpha-enolase antibodies to a 50-kDa polypeptide band resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of M. fermentans membrane or soluble preparations further supports our notion that mycoplasmal surface alpha-enolase is a major Plg binding protein of M. fermentans. polyacrylamide 142-156 plasminogen Homo sapiens 21-24 17883703-9 2007 This was confirmed by sodium dodecylsulfate polyacrylamide gel electrophoresis analysis showing cleavage of alpha(2)-AP by plasmin in the presence of these mAbs. polyacrylamide 44-58 plasminogen Homo sapiens 123-130 7678194-11 1993 The pattern of cross-linked species seen in sodium dodecyl sulfate-polyacrylamide gel electrophoresis reveals that individual plasmin molecules are bound to alpha 2M through one or two cross-links. polyacrylamide 67-81 plasminogen Homo sapiens 126-133 10648407-4 2000 Plasmin (50 nM) decreased the 1-stage clotting activity of F.IX (4 microM) by 80% and the activity of F.IXa (4 microM) by 50% after 30 minutes at 37 degrees C. Plasmin hydrolysis of F.IX yields products of 45, 30, 20, and 14 kd on reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and 2 products of 52 and 14 kd under nonreducing conditions. polyacrylamide 263-277 plasminogen Homo sapiens 0-7 10648407-4 2000 Plasmin (50 nM) decreased the 1-stage clotting activity of F.IX (4 microM) by 80% and the activity of F.IXa (4 microM) by 50% after 30 minutes at 37 degrees C. Plasmin hydrolysis of F.IX yields products of 45, 30, 20, and 14 kd on reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and 2 products of 52 and 14 kd under nonreducing conditions. polyacrylamide 263-277 plasminogen Homo sapiens 160-167 8631822-9 1996 Plasmin yields two fragments of VEGF as indicated by reverse phase high performance liquid chromatography and SDS-polyacrylamide gel electrophoresis: an amino-terminal homodimeric protein containing receptor binding determinants and a carboxyl-terminal polypeptide which bound heparin. polyacrylamide 114-128 plasminogen Homo sapiens 0-7 15202636-8 2004 The proteolytic activity of plasmin by urea-polyacrylamide gel electrophoresis and the white blood cell (WBC) differentials were determined. polyacrylamide 44-58 plasminogen Homo sapiens 28-35 3280426-10 1988 ); of plasminogen have been reported (16) after isoelectric focusing of human plasma in polyacrylamide gels. polyacrylamide 88-102 plasminogen Homo sapiens 6-17 2497995-6 1989 When KW-sct-PA was treated with plasmin, SDS-polyacrylamide gel electrophoresis revealed two bands of Mr 37,000 and 33,000 under reduced conditions. polyacrylamide 45-59 plasminogen Homo sapiens 32-39 1352796-0 1992 Simultaneous diagnosis of coagulation factor XIIA (F13A) and plasminogen (PLG) phenotypes by polyacrylamide gel isoelectric focusing. polyacrylamide 93-107 plasminogen Homo sapiens 74-77 1299319-1 1992 The distribution of Plasminogen (PLG) phenotypes in five populations of Spain (Galicia, Castilla-La Mancha, Castilla-Leon, Extremadura and Western Andalucia) is analysed by means of polyacrylamide gel isoelectric focusing and immunofixation. polyacrylamide 182-196 plasminogen Homo sapiens 20-31 1900515-1 1991 Action of purified human cathepsin B on recombinant single-chain urokinase-type plasminogen activator (pro-uPA) generated enzymatically active two-chain uPA (HMW-uPA), which was indistinguishable by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot from plasmin-generated HMW-uPA and from elastase- or thrombin-generated inactive two-chain urokinase-type plasminogen activator. polyacrylamide 222-236 plasminogen Homo sapiens 80-87 1855784-1 1991 The genetic polymorphism of human plasminogen (PLG) was investigated in Libyans using wide-scale ultrathin-layer polyacrylamide isoelectric focusing with subsequent immunoblotting. polyacrylamide 113-127 plasminogen Homo sapiens 34-45 1855784-1 1991 The genetic polymorphism of human plasminogen (PLG) was investigated in Libyans using wide-scale ultrathin-layer polyacrylamide isoelectric focusing with subsequent immunoblotting. polyacrylamide 113-127 plasminogen Homo sapiens 47-50 2007871-2 1991 In this study, the PLG types were determined by isoelectric focusing in polyacrylamide gels (PAGIF), followed by staining with Coomassie blue. polyacrylamide 72-86 plasminogen Homo sapiens 19-22 11453087-1 1990 The polymorphism of plasminogen (PLG) was analysed by isoelectric focusing on polyacrylamide gels, followed by electroblotting. polyacrylamide 78-92 plasminogen Homo sapiens 33-36 2946579-5 1986 Polyacrylamide/urea/acetic acid gel electrophoresis revealed that the radioiodinated plasminogen bound to plasmin-degraded fibrin was of the Glu form. polyacrylamide 0-14 plasminogen Homo sapiens 85-92 2441753-1 1987 Analysis of plasmin-alpha 2-macroglobulin interactions by polyacrylamide gel electrophoresis showed that both the light and heavy chains of the proteinase have covalent links with the inhibitor. polyacrylamide 58-72 plasminogen Homo sapiens 12-19 2943320-6 1986 Plasmin-catalysed transformation of 125I-labelled Glu-1- to Lys-77-plasminogen is quantified following separation by polyacrylamide gel electrophoresis at pH 3.2. polyacrylamide 117-131 plasminogen Homo sapiens 0-7 3019419-3 1986 Plasmin, pronase, cathepsin D or cathepsin B each degraded the nonglycosylated and control fibrinogens similarly, as evidenced by the release of trichloroacetic acid-soluble radioactivity and by SDS-polyacrylamide gel electrophoresis and autoradiography of plasmic digests. polyacrylamide 199-213 plasminogen Homo sapiens 0-7 2944691-3 1986 This enzyme was identified as plasmin because it displayed an apparent Mr of 90,000 on nonreduced SDS polyacrylamide gel electrophoresis, was able to directly lyse fibrin and the chromogenic substrate H-D-Val-Leu-Lys-p-nitroanilide, and was stable after heating at 56 degrees for 30 min but broke down at 80 degrees. polyacrylamide 102-116 plasminogen Homo sapiens 30-37 2939588-1 1986 The rate of plasmin-catalyzed Glu-plasminogen to Lys-plasminogen conversion was faster in the presence of fibrin than in its absence when assayed by SDS-polyacrylamide gel electrophoresis followed by quantification of stained bands by densitometer. polyacrylamide 153-167 plasminogen Homo sapiens 12-19 6562066-2 1984 This degradation of the plasmin inhibitor, described earlier as "spontaneously" occurring conversion, is shown in dodecyl sulfate polyacrylamide gel electrophoresis, in two-dimensional immunoelectrophoresis and by measuring the kinetics of plasmin inhibition. polyacrylamide 130-144 plasminogen Homo sapiens 24-31 3861032-1 1985 The genetically determined polymorphism of plasminogen (PLG) was analyzed by isoelectric focusing on polyacrylamide gels. polyacrylamide 101-115 plasminogen Homo sapiens 43-54 3861032-1 1985 The genetically determined polymorphism of plasminogen (PLG) was analyzed by isoelectric focusing on polyacrylamide gels. polyacrylamide 101-115 plasminogen Homo sapiens 56-59 6214361-1 1982 A method for separate measurement of the amounts of the native form and partially degraded form of plasminogen and plasmin in human circulating blood was devised based on their different mobilities on disc polyacrylamide gel electrophoresis. polyacrylamide 206-220 plasminogen Homo sapiens 99-106 7076248-1 1982 Genetic polymorphism of human plasminogen in the Japanese population has been described using polyacrylamide gel isoelectric focusing electrophoresis followed by immuno-fixation techniques. polyacrylamide 94-108 plasminogen Homo sapiens 30-41 6454129-1 1981 A commercial preparation of human plasmin (Homolysin), capable of catalyzing the transformation of human growth hormone (hGH) into biologically activated species, was analyzed by electrophoresis and electrofocusing on polyacrylamide gel. polyacrylamide 218-232 plasminogen Homo sapiens 34-41 6454129-4 1981 Polyacrylamide gel electrophoresis of Homolysin in the presence of sodium dodecylsulfate (SDS) yielded 2 subunits which corresponded in molecular weight to the known plasmin subunits. polyacrylamide 0-14 plasminogen Homo sapiens 166-173 145666-1 1977 The proteolysis of purified human fibrinogen, stabilized and non-stabilized fibrin by plasmin were investigated by gel filtration analysis and SDS polyacrylamide electrophoresis of the reaction products. polyacrylamide 147-161 plasminogen Homo sapiens 86-93 7378321-4 1980 In addition, sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) on unreduced samples frequently showed bands similar in mol wt to fragments X, Y and D, and in the reduced samples A alpha and B beta chain degradation, both indicating plasmin activity. polyacrylamide 37-51 plasminogen Homo sapiens 252-259 147811-1 1978 The incubation of human fibrinogen with plasmin gives rise to an early degradation product with a molecular weight of 63,000, calculated by polyacrylamide-gel electrophoresis sodium dodecyl sulfate (PAGE-SDS); this product is resistant to the action of the plasmin for short incubation times and represents 1 +/- 0.2% of the original quantity of fibrinogen. polyacrylamide 140-154 plasminogen Homo sapiens 40-47 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. polyacrylamide 234-248 plasminogen Homo sapiens 118-125 128454-1 1975 A method is described by which the heavy chain of human plasmin, obtained by partial reduction of urokinase-activated plasminogen with 2-mercaptoethanol, is adsorbed on lysine coupled to polyacrylamide. polyacrylamide 187-201 plasminogen Homo sapiens 56-63 59380-12 1975 Indeed plasmin is able to produce such fragments having an antitryptic activity as shown by fibrin/polyacrylamide gel electrophoresis. polyacrylamide 99-113 plasminogen Homo sapiens 7-14 1192601-1 1975 Polyacrylamide (PA) gel electrophoresis in sodium dodecyl sulphate (SDS) has been shown to distinguish between the major components in the plasmin induced lysates of purified crosslinked fibrin and fibrinogen. polyacrylamide 0-14 plasminogen Homo sapiens 139-146 1192601-1 1975 Polyacrylamide (PA) gel electrophoresis in sodium dodecyl sulphate (SDS) has been shown to distinguish between the major components in the plasmin induced lysates of purified crosslinked fibrin and fibrinogen. polyacrylamide 16-18 plasminogen Homo sapiens 139-146 125419-3 1975 When the S-carbamidomethylated hormone was incubated overnight with human plasmin, approximately 95% of the starting material was completely digested, as judged by polyacrylamide gel electrophoresis. polyacrylamide 164-178 plasminogen Homo sapiens 74-81 4248004-0 1970 Heterogeneity of human fibrinogen: possible relation to proteolysis by thrombin and plasmin as studies by SDS-polyacrylamide gel electrophoresis. polyacrylamide 110-124 plasminogen Homo sapiens 84-91