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In vitro evaluation of the haemostatic value of the LFB‐von Willebrand factor concentrate
Author(s) -
Claudine Mazurier
Publication year - 1998
Publication title -
haemophilia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.213
H-Index - 92
eISSN - 1365-2516
pISSN - 1351-8216
DOI - 10.1046/j.1365-2516.1998.0040s3040.x
Subject(s) - von willebrand factor , ristocetin , platelet , glycoprotein , agarose , von willebrand disease , medicine , in vitro , platelet membrane glycoprotein , agarose gel electrophoresis , microbiology and biotechnology , thrombin , biochemistry , immunology , chemistry , biology , dna
The structural and functional studies of the concentrate of von Willebrand factor (vWF) manufactured by LFB have been first performed as part of the preclinical development of this product specially intended for the treatment of von Willebrand disease. The electrophoretic analyses showed the high purity of LFB‐vWF concentrate (specific activity of 100 IU of ristocetin cofactor activity per milligram of protein) and the multimeric pattern attesting the presence of high molecular weight multimeters (≥15‐mers). The measurements of vWF capacity to bind to: (1) platelet glycoprotein (GP) Ib in the presence of ristocetin; (2) GPIIb/IIIa in the presence of thrombin; (3) types I and III collagen; (4) factor VIII (FVIII) gave evidence that the functional activity of purified vWF was similar to that of native plasma vWF. Furthermore the LFB‐vWF concentrate was able to promote platelet adhesion to collagen. The release of the therapeutic batches of this product rely presently on their potency measured with the ristocetin cofactor activity (40–70 IU ml −1 ) and the quantitative evaluation of vWF multimeric distribution studied using electrophoresis in 1.5% agarose. These validated techniques ensure the consistency and haemostatic properties of the different lots of LFB‐vWF concentrate.