PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22781599-4 2012 Compared with WT-VWF, the susceptibility of A1500E mutant VWF to proteolysis by ADAMTS13 was analyzed using SDS-agarose gel VWF multimers analysis. Sepharose 112-119 von Willebrand factor Homo sapiens 58-61 23340442-5 2013 VWF:CB was analyzed with type III collagen and multimer distribution by agarose gel electrophoresis. Sepharose 72-79 von Willebrand factor Homo sapiens 0-6 22239246-3 2012 The VWF multimeric pattern was studied by agarose gel electrophoresis. Sepharose 42-49 von Willebrand factor Homo sapiens 4-7 20889192-2 2010 To improve the sensitivity, precision and efficiency of this assay, we developed and validated a new in-gel infrared fluorescent VWF multimer imaging method to visualize and quantify VWF multimers directly in the agarose gel, thus eliminating electroblotting or autoradiographic steps. Sepharose 213-220 von Willebrand factor Homo sapiens 129-132 21647922-8 2011 In addition, our method has the additional advantage of being able to resolve the triplet structure of platelet vWF multimers, which has not been identified previously through conventional SDS-agarose electrophoresis multimer analysis. Sepharose 193-200 von Willebrand factor Homo sapiens 112-115 20889192-2 2010 To improve the sensitivity, precision and efficiency of this assay, we developed and validated a new in-gel infrared fluorescent VWF multimer imaging method to visualize and quantify VWF multimers directly in the agarose gel, thus eliminating electroblotting or autoradiographic steps. Sepharose 213-220 von Willebrand factor Homo sapiens 183-186 20575033-5 2010 The analysis of VWF multimers generally consists of four steps: (1) electrophoresis of plasma in an agarose gel, (2) either gel fixation or transfer of the electrophoretic protein product to a membrane, (3) immunodetection of the protein, and (4) evaluation of the protein in the gel or membrane. Sepharose 100-107 von Willebrand factor Homo sapiens 16-19 17164493-8 2007 VWD type 2M is featured by the presence of all VWF multimers in a low resolution agarose gel, normal or slightly prolonged BT, decreased RIPA, a poor response of VWF:RCo and a good response of FVIII and VWF:CB to DDAVP and therefore clearly in between dominant type 1 and 2U. Sepharose 81-88 von Willebrand factor Homo sapiens 47-50 19282656-3 2009 The FVIII/VWF complex was purified from a healthy donor"s plasma by affinity chromatography on a Sepharose 4B-Concanavalin A column and was used to determine its capability to interact with erythrocytes and platelets. Sepharose 97-109 von Willebrand factor Homo sapiens 10-13 20093243-0 2010 Analysis of von Willebrand factor multimers by simultaneous high- and low-resolution vertical SDS-agarose gel electrophoresis and Cy5-labeled antibody high-sensitivity fluorescence detection. Sepharose 98-105 von Willebrand factor Homo sapiens 12-33 20093243-2 2010 A novel method for multimer analysis of vWF by 2-chamber, vertical (sodium dodecyl sulfate), agarose gel electrophoresis, designed for comparing discontinuous high- and low-resolving gels for plasma and platelets, followed by Western blotting and high-sensitivity fluorescence detection (HSFD) of cyanine (Cy)5-labeled vWF multimers is presented. Sepharose 93-100 von Willebrand factor Homo sapiens 40-43 19190814-5 2009 The multimeric pattern of VWF was analyzed by SDS-agarose gel electrophoresis. Sepharose 50-57 von Willebrand factor Homo sapiens 26-29 12884737-6 2003 The extent of vWF degradation was assayed by electrophoresis in SDS-agarose gels and immunoblotting. Sepharose 68-75 von Willebrand factor Homo sapiens 14-17 15198879-4 2004 Multimers of vWF in plasma of patients with TTP were also analyzed by SDS-agarose electrophoresis. Sepharose 74-81 von Willebrand factor Homo sapiens 13-16 12513717-3 2002 After confirming by DNA sequencing analysis, the recombinant expression plasmid pQE31-vWF/A1 was constructed and introduced into E. coli M15 strain, then induced by IPTG; the expressed protein was purified with Ni-NTA agarose, identified by Western blotting. Sepharose 218-225 von Willebrand factor Homo sapiens 86-89 12601725-1 2003 Rapid and highly reproducible nonreducing agarose gel electrophoresis (NRAGE) of von Willebrand Factor (vWF) multimers was performed using a thermostated minigel apparatus that monitors and precisely controls internal gel temperature. Sepharose 42-49 von Willebrand factor Homo sapiens 81-102 12601725-1 2003 Rapid and highly reproducible nonreducing agarose gel electrophoresis (NRAGE) of von Willebrand Factor (vWF) multimers was performed using a thermostated minigel apparatus that monitors and precisely controls internal gel temperature. Sepharose 42-49 von Willebrand factor Homo sapiens 104-107 11475150-3 2001 Von Willebrand"s factor (VWF) multimers were assayed with high- and low-resolution sodium dodecyl sulfate (SDS) agarose gels. Sepharose 112-119 von Willebrand factor Homo sapiens 0-23 11535495-6 2001 In this study, the purification of human vWF-cleaving protease from a commercial preparation of factor VIII/vWF concentrate by means of several column chromatographic steps, including 2 steps of heparin-Sepharose column, is reported. Sepharose 203-212 von Willebrand factor Homo sapiens 41-44 11992238-12 2002 The analysis of vWF multimers in the different fractions obtained by affinity chromatography on heparin Sepharose showed that the activity measured both with RCo assay and CBA correlated with the degree of multimerization. Sepharose 104-113 von Willebrand factor Homo sapiens 16-19 11836176-0 2002 Immunostaining of von Willebrand factor multimers on agarose gels and nitrocellulose filters. Sepharose 53-60 von Willebrand factor Homo sapiens 18-39 11836176-1 2002 Human von Willebrand factor (VWF) multimeric analysis is commonly performed by agarose gel electrophoresis, electroblotting, and immunoenzymatic staining; however, high molecular weight (HMW) multimers are poorly transferred on nitrocellulose and should be visualized by direct gel staining with radiolabeled anti-VWF antibody and autoradiography or luminography. Sepharose 79-86 von Willebrand factor Homo sapiens 6-27 11836176-1 2002 Human von Willebrand factor (VWF) multimeric analysis is commonly performed by agarose gel electrophoresis, electroblotting, and immunoenzymatic staining; however, high molecular weight (HMW) multimers are poorly transferred on nitrocellulose and should be visualized by direct gel staining with radiolabeled anti-VWF antibody and autoradiography or luminography. Sepharose 79-86 von Willebrand factor Homo sapiens 29-32 11475150-3 2001 Von Willebrand"s factor (VWF) multimers were assayed with high- and low-resolution sodium dodecyl sulfate (SDS) agarose gels. Sepharose 112-119 von Willebrand factor Homo sapiens 25-28 10830921-4 1999 The patients" multimeric vWF pattern was analyzed by sodium dodecylsulfate (SDS)-agarose-acrylamide electrophoresis, Western blot, and densitometric analysis. Sepharose 81-88 von Willebrand factor Homo sapiens 25-28 11920189-4 2000 We determined the range of vWF concentrations in plasma where the percentage of (125)I-MAb/vWF complexes bound to heparin-agarose beads was constant. Sepharose 122-129 von Willebrand factor Homo sapiens 27-30 11877016-3 2000 Human vWF was purified from blood cryoprecipitate by glycine and NaCl precipitation and subsequent separation on sepharose 4B column. Sepharose 113-125 von Willebrand factor Homo sapiens 6-9 10212199-4 1999 When vWf was immobilized on agarose-linked monoclonal antibody, factor VIII bound to vWf with high affinity, and neither the affinity nor binding site availability was influenced by the presence of 50% plasma. Sepharose 28-35 von Willebrand factor Homo sapiens 5-8 10212199-4 1999 When vWf was immobilized on agarose-linked monoclonal antibody, factor VIII bound to vWf with high affinity, and neither the affinity nor binding site availability was influenced by the presence of 50% plasma. Sepharose 28-35 von Willebrand factor Homo sapiens 85-88 10212199-6 1999 In contrast, when vWf was immobilized on agarose-linked collagen, its affinity for factor VIII was reduced 4-fold, with KD increasing from 0.9 to 3.8 nM. Sepharose 41-48 von Willebrand factor Homo sapiens 18-21 8634427-8 1996 DeltaA2-rvWF effectively displaced previously bound factor VIII, confirming that factor VIII binding to vWF-RU1-Sepharose was reversible. Sepharose 112-121 von Willebrand factor Homo sapiens 9-12 9692396-3 1998 FVIII binding to vWF was measured by capture of patient vWF by polyclonal antibodies on cyanogen bromide-activated Sepharose beads, reaction with recombinant FVIII, and assay of unbound FVIII by clotting methods. Sepharose 115-124 von Willebrand factor Homo sapiens 17-20 9129011-5 1997 The extent of vWF degradation was assayed by electrophoresis in sodium dodecyl sulfate-agarose gels and immunoblotting. Sepharose 87-94 von Willebrand factor Homo sapiens 14-17 9222425-2 1996 vWF antigen (vWFAg)-like protein was obtained by gel filtration of the concentrate on Sepharose 4B. Sepharose 86-98 von Willebrand factor Homo sapiens 0-3 8639781-4 1996 We purified (approximately 10,000-fold) from human plasma a vWF-degrading protease, using chelating Sepharose, hydrophobic interaction chromatography, and gel filtration. Sepharose 100-109 von Willebrand factor Homo sapiens 60-63 8634427-3 1996 Purified or plasma vWF was immobilized with a monoclonal antibody (MoAb RU1) covalently linked to Sepharose (Pharmacia LKB Biotechnology, Uppsala, Sweden). Sepharose 98-107 von Willebrand factor Homo sapiens 19-22 8634427-4 1996 Factor VIII was incubated with vWF-RU1-Sepharose and unbound factor VIII was separated from bound factor VIII by centrifugation. Sepharose 39-48 von Willebrand factor Homo sapiens 31-34 8634427-6 1996 Factor VIII binding to vWF-RU1-Sepharose conformed to the Langmuir model for independent binding sites with a Kd of 0.46 +/- 0.12 nmol/L, and a stoichiometry of 1.3 factor VIII molecules per vWF monomer at saturation, suggesting that each vWF subunit contains a binding site for factor VIII. Sepharose 31-40 von Willebrand factor Homo sapiens 23-26 8634427-6 1996 Factor VIII binding to vWF-RU1-Sepharose conformed to the Langmuir model for independent binding sites with a Kd of 0.46 +/- 0.12 nmol/L, and a stoichiometry of 1.3 factor VIII molecules per vWF monomer at saturation, suggesting that each vWF subunit contains a binding site for factor VIII. Sepharose 31-40 von Willebrand factor Homo sapiens 191-194 8634427-6 1996 Factor VIII binding to vWF-RU1-Sepharose conformed to the Langmuir model for independent binding sites with a Kd of 0.46 +/- 0.12 nmol/L, and a stoichiometry of 1.3 factor VIII molecules per vWF monomer at saturation, suggesting that each vWF subunit contains a binding site for factor VIII. Sepharose 31-40 von Willebrand factor Homo sapiens 191-194 10028315-1 1998 In order to provide patients with von Willebrand disease a factor VIII (FVIII)/von Willebrand factor (vWF) concentrate of reproducible quality, an SDS-agarose gel electrophoresis method has been established to determine the content of the high molecular weight multimers (band 11 and higher) of vWF. Sepharose 151-158 von Willebrand factor Homo sapiens 102-105 9075127-14 1997 Analysis of plasma vWF multimeric pattern by SDS-agarose gel electrophoresis disclosed in four IgAN patients abnormally large vWF multimers that were not documented in PGN subjects. Sepharose 49-56 von Willebrand factor Homo sapiens 19-22 8634427-9 1996 To determine the association rate constant (k(on)) and the dissociation rate constant (k(off)), factor VIII was incubated with vWF-RU1-Sepharose for various time intervals. Sepharose 135-144 von Willebrand factor Homo sapiens 127-130 8634427-11 1996 Similar values were obtained from the dissociation kinetics measured after dilution of preformed factor VIII-vWF-RU1-Sepharose complexes. Sepharose 117-126 von Willebrand factor Homo sapiens 109-112 8555986-2 1995 The biological activity of vWF was measured by the ristocetin cofactor assay and its multimeric structure was assessed by Western immunoblotting after SDS-agarose gel electrophoresis. Sepharose 155-162 von Willebrand factor Homo sapiens 27-30 7890268-4 1994 Analysis of plasma vWf multimeric structure by short-SDS-agarose gel electrophoresis showed an abnormal banding pattern for each vWf oligomer, which was organized as a doublet instead of the normal triplet. Sepharose 57-64 von Willebrand factor Homo sapiens 19-22 8054845-3 1994 However, the Lens culinaris lectin immobilized on Sepharose 4B (LCA-Sepharose) provided a more selective and flexible affinity system for the purification of FVIII/vWF than Concanavalia lectin. Sepharose 50-62 von Willebrand factor Homo sapiens 164-167 8054845-3 1994 However, the Lens culinaris lectin immobilized on Sepharose 4B (LCA-Sepharose) provided a more selective and flexible affinity system for the purification of FVIII/vWF than Concanavalia lectin. Sepharose 50-59 von Willebrand factor Homo sapiens 164-167 8054845-4 1994 Chromatography on LCA-Sepharose of a purified FVIII containing a small proportion of vWF required a weak acidic medium (pH 6.3) and relatively slow kinetics (about 20 cm/h flow rate). Sepharose 22-31 von Willebrand factor Homo sapiens 85-88 7890268-4 1994 Analysis of plasma vWf multimeric structure by short-SDS-agarose gel electrophoresis showed an abnormal banding pattern for each vWf oligomer, which was organized as a doublet instead of the normal triplet. Sepharose 57-64 von Willebrand factor Homo sapiens 129-132 8165633-6 1994 In addition, different fractions with low affinity for ATIII were compared as competitors of 125I-vWF binding to heparin-agarose. Sepharose 121-128 von Willebrand factor Homo sapiens 98-101 8494994-3 1993 The patient"s vWF-multimeric structure on SDS agarose gel electrophoresis was similar to that in normal subjects. Sepharose 46-53 von Willebrand factor Homo sapiens 14-17 8191164-4 1993 These are used to reveal, by autoradiography, the bands of vWF of various molecular weights separated by electrophoresis in agarose gels. Sepharose 124-131 von Willebrand factor Homo sapiens 59-62 8215459-10 1993 Furthermore, when immobilized on Sepharose in a manner which does not compromise essential cationic residues, the vWF domain peptides are effective affinity ligands. Sepharose 33-42 von Willebrand factor Homo sapiens 114-117 8222806-7 1993 In addition to mild loss of the largest multimers, changes in oligomeric composition of plasma vWF were observed in most patients using both agarose and polyacrylamide gel electrophoresis. Sepharose 141-148 von Willebrand factor Homo sapiens 95-98 1581233-2 1992 The circulating highest molecular weight multimers (HMWM) of von Willebrand factor (vWF) were decreased when assessed by SDS-agarose plasma electrophoresis, leading to the diagnosis of type II AvWD. Sepharose 125-132 von Willebrand factor Homo sapiens 84-87 1581233-2 1992 The circulating highest molecular weight multimers (HMWM) of von Willebrand factor (vWF) were decreased when assessed by SDS-agarose plasma electrophoresis, leading to the diagnosis of type II AvWD. Sepharose 125-132 von Willebrand factor Homo sapiens 61-82 1641822-4 1992 Analysis of plasma-vWf multimers by agarose gel electrophoresis consistently demonstrated a subtle decrease in the largest vWf multimers. Sepharose 36-43 von Willebrand factor Homo sapiens 19-22 1641822-4 1992 Analysis of plasma-vWf multimers by agarose gel electrophoresis consistently demonstrated a subtle decrease in the largest vWf multimers. Sepharose 36-43 von Willebrand factor Homo sapiens 123-126 1909351-2 1991 As shown by two-dimensional nonreduced/reduced agarose/polyacrylamide gel electrophoresis, the structure of circulating vWf molecules may deviate from that represented by assemblage of a variable number of identical subunits. Sepharose 47-54 von Willebrand factor Homo sapiens 120-123 2363131-0 1990 Luminographic detection of von Willebrand factor multimers in agarose gels and on nitrocellulose membranes. Sepharose 62-69 von Willebrand factor Homo sapiens 27-48 1996556-3 1991 Low-resolution agarose gel electrophoresis showed a vWF with all size multimers in plasma and platelets. Sepharose 15-22 von Willebrand factor Homo sapiens 52-55 1368084-2 1991 Using conventional NaCl gradient methodology it was found that the order of elution of specific plasma proteins, and the yield of VIII/vWf, varied with the methods used to derivatize the agarose beads. Sepharose 187-194 von Willebrand factor Homo sapiens 135-138 2265247-3 1990 Following immunoisolation and analysis by polyacrylamide or agarose gel electrophoresis, metabolically labeled vWF was found to have incorporated [35S]-sulfate into all secreted multimer species. Sepharose 60-67 von Willebrand factor Homo sapiens 111-114 2084949-0 1990 Multimeric analysis of von Willebrand factor by molecular sieving electrophoresis in sodium dodecyl sulphate agarose gel. Sepharose 109-116 von Willebrand factor Homo sapiens 23-44 2084949-1 1990 We report the development and optimisation of an agarose gel electrophoretic method for the separation and detection of von Willebrand Factor (vWF) multimers. Sepharose 49-56 von Willebrand factor Homo sapiens 120-141 2084949-1 1990 We report the development and optimisation of an agarose gel electrophoretic method for the separation and detection of von Willebrand Factor (vWF) multimers. Sepharose 49-56 von Willebrand factor Homo sapiens 143-146 2107883-5 1990 vWF was immunopurified from releasate or media before and after clotting, and the amount and multimeric pattern of vWF bound was determined after sodium dodecyl sulfate agarose gel electrophoresis. Sepharose 169-176 von Willebrand factor Homo sapiens 115-118 34568727-3 2021 The size distribution of VWF multimers is usually analyzed by SDS-agarose gel electrophoresis followed by immunoblotting. Sepharose 66-73 von Willebrand factor Homo sapiens 25-28 2521276-6 1989 Crossed immunoelectrophoresis and sodium dodecyl sulfate (SDS)-agarose gel electrophoresis revealed that the large vWf multimers were either absent from or relatively decreased in all patients except one. Sepharose 63-70 von Willebrand factor Homo sapiens 115-118 35491445-7 2022 VWF multimer analysis was performed using SDS-agarose electrophoresis. Sepharose 46-53 von Willebrand factor Homo sapiens 0-3 2510350-8 1989 Analysis of plasma vWF multimer patterns by 1.4% agarose electrophoresis in 0.1% SDS revealed excessive amounts of large, medium and small size multimers in the PIH patients. Sepharose 49-56 von Willebrand factor Homo sapiens 19-22 2496614-7 1989 Prior to treatment, there was a uniform reduction of all the multimers of plasma vWF in sodium dodecyl sulfate agarose gel electrophoresis. Sepharose 111-118 von Willebrand factor Homo sapiens 81-84 34105490-3 2021 The cleavage products of vWF polymer by wild-type or mutant ADAMTS13 under denaturing condition or shear stress were separated by 1% SeaKem HGT agarose gel and detected by Western blot. Sepharose 144-151 von Willebrand factor Homo sapiens 25-28 2506947-10 1989 Sodium dodecyl sulfate (SDS) 1.4% agarose gel electrophoresis showed that all multimers of vWF were present in both patients. Sepharose 34-41 von Willebrand factor Homo sapiens 91-94 2506947-13 1989 The qualitative abnormality of vWF in both patients was associated with a subtle alteration of the multimeric structure by SDS 3% agarose gel electrophoresis in which the two central subbands of the quintuplet of individual oligomers were undetectable or poorly visible. Sepharose 130-137 von Willebrand factor Homo sapiens 31-34 2455942-0 1988 Chromatography of the VIII/vWF complex on dextran sulphate sepharose. Sepharose 59-68 von Willebrand factor Homo sapiens 27-30 3266380-2 1988 Plasma vWF was hydrolysed by S aureus V-8 protease (V-8 protease) and the cleaved fragments separated by SDS-agarose gel electrophoresis followed by staining with 125I-labeled polyclonal or monoclonal antibodies against vWF and autoradiography. Sepharose 109-116 von Willebrand factor Homo sapiens 7-10 2448895-0 1987 Chromatography of vWf on dextran sulphate sepharose. Sepharose 42-51 von Willebrand factor Homo sapiens 18-21 3126793-5 1988 In the two patients, the highest molecular weight multimers (HMWM) of vWf were absent when assessed by sodium dodecyl-sulphate agarose plasma electrophoresis. Sepharose 127-134 von Willebrand factor Homo sapiens 70-73 3124306-5 1988 Aggregation of the vWf molecule, detected by altered mobility in crossed immunoelectrophoresis and multimeric analysis in SDS agarose gels, occurred in heated intermediate-purity concentrates but not in fibrinogen-poor concentrates. Sepharose 126-133 von Willebrand factor Homo sapiens 19-22 3121600-4 1987 In contrast, when analyzed by agarose/sodium dodecyl sulfate-polyacrylamide gel electrophoresis, vWF consisted of a population of greater than 10 multimers derived from a 270-kDa monomer. Sepharose 30-37 von Willebrand factor Homo sapiens 97-100 2448895-1 1987 A relatively simple and reproducible chromatographic separation using Dextran Sulphate (DS) Agarose is described for the purification of vWf:Ag from cryoprecipitate or plasma source material. Sepharose 92-99 von Willebrand factor Homo sapiens 137-140 2448895-6 1987 DS sepharose chromatography offers an excellent method for the purification of 125I-vWf since all the viable label is resolved from excess free radiolabel and denatured protein. Sepharose 3-12 von Willebrand factor Homo sapiens 84-87 3497849-1 1987 A fast-migrating precipitin peak which showed a reaction of partial immunochemical identity with the major von Willebrand factor (vWf) component was detected by crossed immunoelectrophoresis in agarose gel in plasma but not in platelets from a patient with type IIA von Willebrand"s disease (vWD). Sepharose 194-201 von Willebrand factor Homo sapiens 107-128 3028536-3 1987 During the third trimester of pregnancy, her platelet counts dropped to 20,000 to 30,000/microL, and an increase in the intermediate-sized vWF multimers was seen on agarose gel electrophoresis. Sepharose 165-172 von Willebrand factor Homo sapiens 139-142 3497849-1 1987 A fast-migrating precipitin peak which showed a reaction of partial immunochemical identity with the major von Willebrand factor (vWf) component was detected by crossed immunoelectrophoresis in agarose gel in plasma but not in platelets from a patient with type IIA von Willebrand"s disease (vWD). Sepharose 194-201 von Willebrand factor Homo sapiens 130-133 3030393-7 1986 The factor VIIIdes-797-1562 variant also bound to von Willebrand factor (vWF) immobilized on Sepharose. Sepharose 93-102 von Willebrand factor Homo sapiens 50-71 3030393-7 1986 The factor VIIIdes-797-1562 variant also bound to von Willebrand factor (vWF) immobilized on Sepharose. Sepharose 93-102 von Willebrand factor Homo sapiens 73-76 3487353-2 1986 However, in contrast to the latter two disorders in which the larger vWF multimers are absent in plasma, the entire range of vWF multimers was observed in the patients" plasma after sodium dodecyl sulfate-agarose gel electrophoresis, and all vWF multimers (including the largest) were present in the same proportion as in normal plasma and type I vWD. Sepharose 205-212 von Willebrand factor Homo sapiens 125-128 3487353-2 1986 However, in contrast to the latter two disorders in which the larger vWF multimers are absent in plasma, the entire range of vWF multimers was observed in the patients" plasma after sodium dodecyl sulfate-agarose gel electrophoresis, and all vWF multimers (including the largest) were present in the same proportion as in normal plasma and type I vWD. Sepharose 205-212 von Willebrand factor Homo sapiens 125-128 3520939-2 1986 The method is based upon: 1) Separation of the vWF multimers by SDS-agarose electrophoresis, 2) Subsequent blotting of the vWF multimers onto nitrocellulose, 3) Immunolocalization and visualization of the vWF pattern by the sequential incubation of the blot with primary vWF antiserum, peroxidase- or beta-galactosidase-conjugated secondary antibodies and a relevant chromogenic substrate. Sepharose 68-75 von Willebrand factor Homo sapiens 47-50 3486890-6 1986 We isolated individual vWf oligomer species from the agarose gel bands and show that vWf minor, or satellite, species differ from major species in subunit composition. Sepharose 53-60 von Willebrand factor Homo sapiens 23-26 3877533-8 1985 Analysis of vWF multimeric structure by agarose gel electrophoresis, including a newly developed high-resolution technique, demonstrated that the main band of each multimer was present, but a second, well-defined band always seen in normal individuals was missing in the patients. Sepharose 40-47 von Willebrand factor Homo sapiens 12-15 3484979-1 1986 We identified a consecutive series of 12 children with noncyanotic congenital cardiac lesions with loss of the largest plasma von Willebrand factor (vWF) multimers determined by SDS-agarose electrophoresis. Sepharose 182-189 von Willebrand factor Homo sapiens 126-147 3484979-1 1986 We identified a consecutive series of 12 children with noncyanotic congenital cardiac lesions with loss of the largest plasma von Willebrand factor (vWF) multimers determined by SDS-agarose electrophoresis. Sepharose 182-189 von Willebrand factor Homo sapiens 149-152 3486491-0 1986 Improved characterization of plasma von Willebrand factor heterogeneity when using 2.5% agarose gel electrophoresis. Sepharose 88-95 von Willebrand factor Homo sapiens 36-57 2936763-6 1986 When analyzed by polyacrylamide gel electrophoresis and Sepharose CL6B chromatography, the 440,000-D vWF oligomer is a dimer of the 220,000 subunit of fully reduced native vWF. Sepharose 56-65 von Willebrand factor Homo sapiens 101-104 3486491-3 1986 By using a 2.5% mixture of two selected agaroses, a single electrophoretic analysis of plasma clearly reveals the extreme complexity of the molecular forms of circulating vWF: each multimeric unit of plasma vWF may be separated into five bands, the central one being predominant. Sepharose 40-48 von Willebrand factor Homo sapiens 171-174 3929829-2 1985 In addition, SDS-agarose gel electrophoresis demonstrated alterations of the von Willebrand factor (vWF) multimeric structure. Sepharose 17-24 von Willebrand factor Homo sapiens 77-98 3929829-2 1985 In addition, SDS-agarose gel electrophoresis demonstrated alterations of the von Willebrand factor (vWF) multimeric structure. Sepharose 17-24 von Willebrand factor Homo sapiens 100-103 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 von Willebrand factor Homo sapiens 39-42 3875078-2 1985 Micro-injection of specific polyA+ RNA fractions in Xenopus laevis oocytes provoked the synthesis of a vWF-like product which could be detected with an immunoradiometric assay relying on Sepharose-linked monoclonal anti-vWF IgG and different radiolabeled monoclonal anti-vWF IgGs. Sepharose 187-196 von Willebrand factor Homo sapiens 103-106 6432075-2 1984 All the multimers of vWF:Ag could be seen in the 1.6% SDS-agarose gel electrophoresis patterns of plasma and platelet lysates. Sepharose 58-65 von Willebrand factor Homo sapiens 21-24 6239876-5 1984 All multimers of unreduced carbohydrate-modified von Willebrand factor migrated more rapidly in SDS-agarose, but the triplet pattern of individual multimers was unchanged. Sepharose 100-107 von Willebrand factor Homo sapiens 49-70 2981585-2 1985 By sodium dodecylsulfate-agarose gel electrophoresis, native platelet vWF contained some multimers that were larger than those characteristic of plasma vWF. Sepharose 25-32 von Willebrand factor Homo sapiens 70-73 6426548-4 1984 Examination of the multimeric structure of the remaining unadsorbed FVIII/vWF protein by agarose gel electrophoresis and autoradiography showed that the largest multimers had been adsorbed to the collagen. Sepharose 89-96 von Willebrand factor Homo sapiens 74-77 6607757-10 1984 By SDS-agarose electrophoresis and radioimmunoblotting, the vWF within the cytosol of the endothelial cells was found to possess a multimeric pattern similar to that found for either purified plasma vWF or vWF released into media overlying endothelial cell cultures. Sepharose 7-14 von Willebrand factor Homo sapiens 60-63 6605165-5 1983 In the propositus, analysis of vWF multimers in plasma on 1.6% sodium dodecyl sulfate (SDS) agarose revealed that there were no larger multimers and there was a relative increase of the smallest multimer. Sepharose 92-99 von Willebrand factor Homo sapiens 31-34 6605344-2 1983 A quantitative recovery of high Mr vWf oligomers has been obtained after binding to a monoclonal anti-vWf-Sepharose adduct. Sepharose 106-115 von Willebrand factor Homo sapiens 35-38 6605344-2 1983 A quantitative recovery of high Mr vWf oligomers has been obtained after binding to a monoclonal anti-vWf-Sepharose adduct. Sepharose 106-115 von Willebrand factor Homo sapiens 102-105 6815213-4 1982 A population of multimeric FVIII/vWF species ranging in molecular weight from 1 to 5 million daltons and differing in size alternately by one and two subunits was observed on SDS-2% polyacrylamide-0.5% agarose gel electrophoresis. Sepharose 202-209 von Willebrand factor Homo sapiens 33-36 6411111-0 1983 Electroblotting of factor VIII/von Willebrand factor multimers after electrophoresis in SDS-agarose gel, discontinuous buffer system. Sepharose 92-99 von Willebrand factor Homo sapiens 31-52 6982283-1 1982 A variant of von Willebrand"s disease has been identified in which sodium dodecyl sulfate agarose electrophoresis provides evidence that the von Willebrand factor present is structurally abnormal. Sepharose 90-97 von Willebrand factor Homo sapiens 141-162 6600402-0 1983 Isoelectric focusing of human von Willebrand factor in urea-agarose gels. Sepharose 60-67 von Willebrand factor Homo sapiens 30-51 6600402-1 1983 An analytical technique has been developed for the isoelectric focusing (IEF) of plasma von Willebrand factor (vWF) in agarose gels containing urea. Sepharose 119-126 von Willebrand factor Homo sapiens 88-109 6600402-1 1983 An analytical technique has been developed for the isoelectric focusing (IEF) of plasma von Willebrand factor (vWF) in agarose gels containing urea. Sepharose 119-126 von Willebrand factor Homo sapiens 111-114 408379-6 1977 When thrombin-activated FVIII/vWF protein was filtered on 4% agarose in 0.15 M NaCl, there was considerable inactivation of FVIII procoagulant activity; however, the procoagulant activity that did remain eluted in the void volume. Sepharose 61-68 von Willebrand factor Homo sapiens 30-33 408379-1 1977 When Factor VIII/von Willebrand factor (FVIII/vWF) protein is rechromatographed on 4% agarose in 0.25 M CaCl(2), the protein and vWF activity appear in the void volume, but most of the FVIII procoagulant activity elutes later. Sepharose 86-93 von Willebrand factor Homo sapiens 17-38 408379-1 1977 When Factor VIII/von Willebrand factor (FVIII/vWF) protein is rechromatographed on 4% agarose in 0.25 M CaCl(2), the protein and vWF activity appear in the void volume, but most of the FVIII procoagulant activity elutes later. Sepharose 86-93 von Willebrand factor Homo sapiens 46-49 408379-1 1977 When Factor VIII/von Willebrand factor (FVIII/vWF) protein is rechromatographed on 4% agarose in 0.25 M CaCl(2), the protein and vWF activity appear in the void volume, but most of the FVIII procoagulant activity elutes later. Sepharose 86-93 von Willebrand factor Homo sapiens 129-132 408379-2 1977 Recent evidence suggests that the delayed FVIII procoagulant activity is a proteolytically modified form of FVIII/vWF protein that filters anomalously from agarose in 0.25 M CaCl(2). Sepharose 156-163 von Willebrand factor Homo sapiens 114-117 408379-7 1977 In contrast, when thrombin-activated FVIII/vWF protein was filtered in 0.25 M CaCl(2), the FVIII procoagulant activity eluted well after the void volume and remained activated for 6 h. The procoagulant peak isolated by filtering nonthrombin-activated FVIII/vWF protein on agarose in 0.25 M CaCl(2) was compared to that isolated from thrombin-activated FVIII/vWF protein. Sepharose 272-279 von Willebrand factor Homo sapiens 43-46 1080491-5 1975 In one patient the Factor VIII/von Willebrand factor protein eluted from Sepharose 4B in a position and distribution identical to normal with normal levels of procoagulant activity and antigen. Sepharose 73-82 von Willebrand factor Homo sapiens 31-52 1080491-7 1975 In the second patient the peak of Factor VIII/von Willebrand factor protein, antigen, and procoagulant activity eluted from a Sepharose 4B column with an estimated molecular weight of approximately half that of normal. Sepharose 126-135 von Willebrand factor Homo sapiens 46-67 4542944-7 1973 This finding, in addition to the observation that agarose gel chromatography fractions that have VIII(AHF) procoagulant activity also have VIII(VWF) activity, strongly suggests that the von Willebrand factor is associated with the factor VIII molecule. Sepharose 50-57 von Willebrand factor Homo sapiens 186-207 28729354-9 2017 vWF multimers and degradation fragments were quantified with agarose and polyacrylamide gel electrophoresis and immunoblotting. Sepharose 61-68 von Willebrand factor Homo sapiens 0-3 31393047-4 2019 METHODS: Covalent complexes between ADAMTS13 and VWF were determined by agarose gel electrophoresis under nonreducing conditions. Sepharose 72-79 von Willebrand factor Homo sapiens 49-52 30731387-2 2019 Analysis of von Willebrand factor (VWF) multimer distribution (VWF:MD) is essential to properly classify and treat different types of VWD, and it is performed using a SDS agarose gel electrophoresis followed by Western blotting, a handmade technique that demands days to be completed and requires skillful execution. Sepharose 171-178 von Willebrand factor Homo sapiens 12-33 30731387-2 2019 Analysis of von Willebrand factor (VWF) multimer distribution (VWF:MD) is essential to properly classify and treat different types of VWD, and it is performed using a SDS agarose gel electrophoresis followed by Western blotting, a handmade technique that demands days to be completed and requires skillful execution. Sepharose 171-178 von Willebrand factor Homo sapiens 35-38 30731387-2 2019 Analysis of von Willebrand factor (VWF) multimer distribution (VWF:MD) is essential to properly classify and treat different types of VWD, and it is performed using a SDS agarose gel electrophoresis followed by Western blotting, a handmade technique that demands days to be completed and requires skillful execution. Sepharose 171-178 von Willebrand factor Homo sapiens 63-66 29126301-20 2017 Testing the functional activity of VWF, utilizes the drug ristocetin.The state of multimerization of VWF is important and is assessed by electrophoresis on agarose gels. Sepharose 156-163 von Willebrand factor Homo sapiens 35-38 29126301-20 2017 Testing the functional activity of VWF, utilizes the drug ristocetin.The state of multimerization of VWF is important and is assessed by electrophoresis on agarose gels. Sepharose 156-163 von Willebrand factor Homo sapiens 101-104 27040683-6 2016 In a patient with Waldenstrom"s macroglobulinemia and severe depletion of plasma VWF, multimer analysis indicated association of the IgM paraprotein with VWF before, but not after plasmapheresis, resulting in destruction of the agarose gel and a characteristically distorted band structure of VWF multimers. Sepharose 228-235 von Willebrand factor Homo sapiens 154-157 27040683-6 2016 In a patient with Waldenstrom"s macroglobulinemia and severe depletion of plasma VWF, multimer analysis indicated association of the IgM paraprotein with VWF before, but not after plasmapheresis, resulting in destruction of the agarose gel and a characteristically distorted band structure of VWF multimers. Sepharose 228-235 von Willebrand factor Homo sapiens 154-157