PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6815213-1 1982 The structure of native and progressively reduced human factor VIII/von Willebrand factor (FVIII/vWF) was examined by electron microscopy and SDS gel electrophoresis and then correlated with its biological activities. Sodium Dodecyl Sulfate 142-145 coagulation factor VIII Homo sapiens 91-96 6982084-1 1982 The multimeric structure of platelet factor VIII/von Willebrand factor (FVIII/vWF) in cell extracts and in collagen and thrombin releasates has been analyzed by SDS polyacrylamide gel electrophoresis followed by detection with 125I-anti-FVIII/vWF. Sodium Dodecyl Sulfate 161-164 coagulation factor VIII Homo sapiens 72-77 6815213-5 1982 With progressive reduction of disulfide bonds by dithiothreitol (DTT), the electron microscopic size of FVIII/vWF decreased in parallel with increased electrophoretic mobility on SDS-agarose gels; between 0.1 and 0.5 mM DTT its structure changed from predominantly fibrillar species to large nodular forms. Sodium Dodecyl Sulfate 179-182 coagulation factor VIII Homo sapiens 104-109 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. Sodium Dodecyl Sulfate 175-178 coagulation factor VIII Homo sapiens 27-32 23517528-6 2013 SDS-PAGE analysis revealed that APCC sequentially proteolyzed the heavy chain of FVIII at Arg(372) and Arg(740) , followed by cleavage at Arg(336) . Sodium Dodecyl Sulfate 0-3 coagulation factor VIII Homo sapiens 81-86 315413-2 1979 FVIII/vWF was isolated by preparative counter immunoelectrophoresis directly from plasma using antibody to Factor VIII-related antigen, reduced in sodium dodecyl sulfate in the presence of urea, and electrophoresed in 5% polyacrylamide gels to separate the FVIII/vWF subunit from other proteins. Sodium Dodecyl Sulfate 147-169 coagulation factor VIII Homo sapiens 0-5 29614522-4 2018 SDS-PAGE demonstrated that the purified inhibitor IgG recognizing residues 373-562 blocked FXa cleavage at Arg372 in FVIII, and surface-plasmon resonance (SPR)-based assays showed that intact A2 subunit directly bound to FX (Kd; 63 nM). Sodium Dodecyl Sulfate 0-3 coagulation factor VIII Homo sapiens 117-122 23813406-5 2013 SDS-PAGE and Western blot analysis confirmed the expression of factor VIII light chain protein. Sodium Dodecyl Sulfate 0-3 coagulation factor VIII Homo sapiens 63-74 8221239-4 1993 For this purpose, the different active forms of FVIII were separated by FPLC and characterized by SDS-PAGE. Sodium Dodecyl Sulfate 98-101 coagulation factor VIII Homo sapiens 48-53 18337255-4 2008 IgG Abs to FVIII from HA patients formed stable immune complexes with E-FVIII and E-C2 that were refractory to dissociation by SDS treatment and boiling, procedures that dissociate noncovalent Ab-antigen complexes. Sodium Dodecyl Sulfate 127-130 coagulation factor VIII Homo sapiens 11-16 12689334-6 2003 Furthermore, SDS/PAGE and Western-blot experiments showed that the specific appearance of the 44 kDa A2 domain on cleavage of the FVIII Arg(372)-Ser(373) peptide bond was delayed significantly in the presence of either GpIbalpha 1-282 or GpIb 268-282 peptide. Sodium Dodecyl Sulfate 13-16 coagulation factor VIII Homo sapiens 130-135 11916079-5 2002 Furthermore, analysis by SDS-PAGE showed that all alloantibodies inhibited FVIII proteolytic cleavage by FXa independently of phospholipid. Sodium Dodecyl Sulfate 25-28 coagulation factor VIII Homo sapiens 75-80 9427707-6 1998 Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of immunoprecipitated FVIII protein radiolabeled in COS-1 cells showed that all CRM-positive mutant proteins were synthesized and secreted into the medium at rates similar to wild-type FVIII. Sodium Dodecyl Sulfate 0-22 coagulation factor VIII Homo sapiens 89-94 7893714-4 1995 Circular dichroism spectra indicate that fVIII2303-24 is predominantly a random coil in aqueous solution but adopts a predominantly helical conformation upon interaction with SDS micelles. Sodium Dodecyl Sulfate 175-178 coagulation factor VIII Homo sapiens 41-46 1905722-5 1991 The proteolytic fragmentation of fVIII by thrombin was evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and was not different between human and porcine fVIII, yielding previously identified bands corresponding to fragments A1, A2, A3-C1-C2, and the B domain. Sodium Dodecyl Sulfate 68-90 coagulation factor VIII Homo sapiens 33-38 2496750-2 1989 Analysis of the proteolyic cleavage of fVIII by thrombin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) identifies three fragments designated fVIIIA1, fVIIIA2, and fVIIIA3-C1-C2 with fragment(s) derived from the B domain being difficult to visualize. Sodium Dodecyl Sulfate 60-82 coagulation factor VIII Homo sapiens 39-44 2496750-2 1989 Analysis of the proteolyic cleavage of fVIII by thrombin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) identifies three fragments designated fVIIIA1, fVIIIA2, and fVIIIA3-C1-C2 with fragment(s) derived from the B domain being difficult to visualize. Sodium Dodecyl Sulfate 119-122 coagulation factor VIII Homo sapiens 39-44 2496750-8 1989 This agrees well with the summed apparent molecular weights of fVIIIA1, fVIIIA2, and fVIIIA3-C1-C2 calculated from SDS-PAGE analysis (148,000) or from the amino acid sequence of human fVIII (159,000). Sodium Dodecyl Sulfate 115-118 coagulation factor VIII Homo sapiens 63-68 3149045-7 1988 A haemophilic antibody specific for epitopes of the light chain of FVIII, employed in immunoisolation of VIII:Ag in lysate of human hepatocytes, extracted a polypeptide pattern that was studied in a reduced SDS-PAGE electrophoresis gel and compared to that of immunoisolate from normal plasma. Sodium Dodecyl Sulfate 207-210 coagulation factor VIII Homo sapiens 67-72 3150544-5 1988 FVIII delta II has the following properties: (i) it exhibits FVIII procoagulant activity; (ii) it is expressed at 5-fold higher levels than is the complete molecule in comparable systems; (iii) it migrates for the most part as a single major band on SDS-PAGE, in contrast to the complete molecule; (iv) it is activated to a greater extent by thrombin than is either rFVIII or pdFVIII; and (v) it retains the ability to bind von Willebrand factor (vWf). Sodium Dodecyl Sulfate 250-253 coagulation factor VIII Homo sapiens 0-5 1899619-2 1991 Thrombin treatment and SDS-PAGE analysis of the purified recombinant FVIII (rFVIII) revealed a striking difference from plasma-derived FVIII (pFVIII). Sodium Dodecyl Sulfate 23-26 coagulation factor VIII Homo sapiens 69-74