Isolation of Small Molecular Forms of Factor VIII/von Willebrand Factor from Plasma

Perret, Beat A.; Furlan, Miha; Beck, Eugene A.

doi:10.1159/000215077

Cited by 4 publications

(4 citation statements)

References 11 publications

(12 reference statements)

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“…Several chromatographic methods have been tested at the bench scale to isolate either vWF or the FVIII/vWF mixture. These procedures involved size exclusion [8], or ion-exchange on aminohexyl- [9] or dextran sulfate- [lo] agarose resins. The drawbacks to using size exclusion chromatography were low protein resolution and lack of stability possible due to protease contamination.…”

Section: Introductionmentioning

confidence: 99%

Chromatographic Preparation of a Therapeutic Highly Purified von Willebrand Factor Concentrate from Human Cryoprecipitate

Burnouf-Radosevich¹,

Burnouf²

1992

Vox Sanguinis

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A therapeutic highly purified von Willebrand factor (vWF) concentrate has been prepared from cryoprecipitate by a three-step chromatographic procedure. After solvent/detergent treatment to inactivate viruses, the cryoprecipitate solution was chromatographed on DEAE-fractogel TSK 650 M to separate vWF from most cryoprecipitate proteins, including factor VIII (FVIII) and fibrinogen. A second DEAE-fractogel TSK 650 M was then performed to further purify vWF and to allow concentrating it to over 100 U ristocetin cofactor activity/ml. The last step on immobilized gelatin removed fibronectin and increased the purity of vWF. vWF was recovered with about 18 and 40% yield in antigen and collagen-binding (CB) activity, respectively, from cryoprecipitate. vWF was obtained in an essentially pure state corresponding to a purification factor of over 10,000-fold from plasma. Immunonephelometric and SDS-PAGE analyses of the concentrate did not reveal any detectable cryoprotein contaminants, especially fibrinogen, fibronectin, immunoglobulins and albumin. The content in intermediate- and high-molecular-weight multimers in the concentrate was similar or higher than that of plasma, as the ion-exchanger selectively favored the binding and concentration of the larger multimeric forms while reducing the amount of the smaller forms with abnormal structure and low activity. Other characteristics of the concentrate included a CB activity to antigen ratio of 1.69 and a high capacity (86%) to correct platelet adhesion in a perfusion system. Clinical use of this standardized vWF concentrate has been shown to be efficacious in the treatment of vWF patients.

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Section: Introductionmentioning

confidence: 99%

Chromatographic Preparation of a Therapeutic Highly Purified von Willebrand Factor Concentrate from Human Cryoprecipitate

Burnouf-Radosevich¹,

Burnouf²

1992

Vox Sanguinis

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“…For example, Perret and colleagues attempted to create a VWF:RCo-like assay using collagen. 37 They found that insoluble collagen from bovine aorta was able to agglutinate washed fixed platelets in the presence of VWF, similarly with the VWF:RCo assay. Their “VWF-collagen cofactor” activity assay showed good correlation ( r = 0.91) with their VWF:RCo assay using 65 plasma samples containing various concentrations of VWF.…”

Section: A History Of the Von Willebrand Factor Collagen-binding Assaymentioning

confidence: 79%

“…The initial reports used methods that were complex or time consuming, or like VWF:RCo. 37 38 Several workers, including us, have described flow-based VWF:CB assays, 220 289 or surface plasmon resonance-based VWF:CB assay. 83 However, none of these have ever taken off, and the most often used method remains the ELISA method, which have devolved from the original method of Brown and Bosak.…”

Section: Discussionmentioning

confidence: 99%

The Role of the von Willebrand Factor Collagen-Binding Assay (VWF:CB) in the Diagnosis and Treatment of von Willebrand Disease (VWD) and Way Beyond: A Comprehensive 36-Year History

Favaloro

2023

Semin Thromb Hemost

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The von Willebrand factor (VWF) collagen binding (VWF:CB) assay was first reported for use in von Willebrand diagnostics in 1986, by Brown and Bosak. Since then, the VWF:CB has continued to be used to help diagnose von Willebrand disease (VWD) (correctly) and also to help assign the correct subtype, as well as to assist in the monitoring of VWD therapy, especially desmopressin (DDAVP). However, it is important to recognize that the specific value of any VWF:CB is predicated on the use of an optimized VWF:CB, and that not all VWF:CB assays are so optimized. There are some good commercial assays available, but there are also some “not-so-good” commercial assays available, and these may continue to give the VWF:CB “a bad reputation.” In addition to VWD diagnosis and management, the VWF:CB found purpose in a variety of other applications, from assessing ADAMTS13 activity, to investigation into acquired von Willebrand syndrome (especially as associated with use of mechanical circulatory support or cardiac assist devices), to assessment of VWF activity in disease states in where an excess of high-molecular-weight VWF may accumulate, and lead to increased (micro)thrombosis risk (e.g., coronavirus disease 2019, thrombotic thrombocytopenic purpura). The VWF:CB turns 37 in 2023. This review is a celebration of the utility of the VWF:CB over this nearly 40-year history.

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“…These procedures involved size exclusion [8], or ion-exchange on aminohexyl- [9] or dextran sulfate- [10] agarose resins. The drawbacks to using size exclusion chromatography were low protein resolution and lack of stability possible due to protease contamination.…”

Section: Introductionmentioning

confidence: 99%

Chromatographic Preparation of a Therapeutic Highly Purified von Willebrand Factor Concentrate from Human Cryoprecipitate

Burnouf-Radosevich¹,

Burnouf²

1992

Vox Sanguinis

View full text Add to dashboard Cite

A therapeutic highly purified von Willebrand factor (vWF) concentrate has been prepared from cryoprecipitate by a three-step chromatographic procedure. After solvent/detergent treatment to inactivate viruses, the cryoprecipitate solution was chromatographed on DEAE-fractogel TSK 650 M to separate vWF from most cryoprecipitate proteins, including factor Vili (FVIII) and fibrinogen. A second DEAE-fractogel TSK 650 M was then performed to further purify vWF and to allow concentrating it to over 100 U ristocetin cofactor activity/ml. The last step on immobilized gelatin removed fibronectin and increased the purity of vWF. vWF was recovered with about 18 and 40% yield in antigen and collagen-binding (CB) activity, respectively, from cryoprecipitate. vWF was obtained in an essentially pure state corresponding to a purification factor of over 10,000-fold from plasma. Immunonephelometric and SDS-PAGE analyses of the concentrate did not reveal any detectable cryoprotein contaminants, especially fibrinogen, fibronectin, immunoglobulins and albumin. The content in intermediate- and high-molecular-weight multimers in the concentrate was similar or higher than that of plasma, as the ion-exchanger selectively favored the binding and concentration of the larger multimeric forms while reducing the amount of the smaller forms with abnormal structure and low activity. Other characteristics of the concentrate included a CB activity to antigen ratio of 1.69 and a high capacity (86%) to correct platelet adhesion in a perfusion system. Clinical use of this standardized vWF concentrate has been shown to be efficacious in the treatment of vWF patients.

show abstract

Isolation of Small Molecular Forms of Factor VIII/von Willebrand Factor from Plasma

Cited by 4 publications

References 11 publications

Chromatographic Preparation of a Therapeutic Highly Purified von Willebrand Factor Concentrate from Human Cryoprecipitate

Chromatographic Preparation of a Therapeutic Highly Purified von Willebrand Factor Concentrate from Human Cryoprecipitate

The Role of the von Willebrand Factor Collagen-Binding Assay (VWF:CB) in the Diagnosis and Treatment of von Willebrand Disease (VWD) and Way Beyond: A Comprehensive 36-Year History

Chromatographic Preparation of a Therapeutic Highly Purified von Willebrand Factor Concentrate from Human Cryoprecipitate

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