Standardization of the One-stage Assay for Factor VIII (Antihemophilic Factor)

Zacharski, Leo R.; Rosenstein, Robert

doi:10.1093/ajcp/70.2.280

Cited by 25 publications

(13 citation statements)

References 14 publications

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“…It is well documented that a number of preanalytical var iables may affect the factor assay results, such as the clot detection methods, the technical staff, and the data deduc tion methodology [9][10][11]. Analytical parameters, such as buffer systems, aPTT reagent, substrate plasma, and refer ence standard, are also major determinants of assay preci sion and accuracy [11][12][13][14][15], Consequently, to assess profi ciency of the CRCS Blood Services Centres and to set per formance standards it was necessary to implement external quality assurance scheme surveys by the NRL.…”

Section: Discussionmentioning

confidence: 99%

Proficiency Testing of Factor VIII:C Activitiy Assays at the Canadian Red Cross Society National Reference Laboratory

Wasi¹,

Murray²,

Gill³

1994

Vox Sanguinis

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A national proficiency testing program has been established to monitor the accuracy and precision of factor VIII:C (FVIII:C) assays performed at the various Blood Services Centres of the Canadian Red Cross Society involved in the collection and processing of either donor blood designated for component production or plasma destined for fractionation. This paper describes the preparation, design, and results of the first four exercises involving 19 laboratories. The exercices were designed to allow the investigation of intralaboratory variability between replicate samples and precision of assays as well as the causes of interlaboratory variability. The implementation of this program has led to improved precision and interlaboratory agreement on FVIII;C assays. These improvements were achieved mainly as a result of a modification in the method for sample dilution, an increase in both replicate testing of the same sample and the number of sample dilutions, and a reduction in the number of reagent systems used by various centres.

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Section: Discussionmentioning

confidence: 99%

Proficiency Testing of Factor VIII:C Activitiy Assays at the Canadian Red Cross Society National Reference Laboratory

Wasi¹,

Murray²,

Gill³

1994

Vox Sanguinis

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“…The FVIII assay was performed as described in the literature, 27 with minor modifications. Blood samples were collected in microfuge tubes containing sodium citrate.…”

Section: Coagulation Assaymentioning

confidence: 99%

The therapeutic effect of bone marrow–derived liver cells in the phenotypic correction of murine hemophilia A

Yadav

Kanjirakkuzhiyil

Kumar

et al. 2009

Blood

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“…Eluted fractions were pooled and dialyzed against TBS and kept at 4°C until used. FVIII coagulant activity was measured with activated partial thromboplastin time (aPTT) (Neothromtin, Behringwerke A.G., Marburg, Germany) (Zacharski and Rosenstein 1978), and protein quantification was performed with the pyrogallol/molybdate complex from BioSystem S.A (Barcelona, Spain) (Yoshikazu et al 1983), using bovine serum albumin as standard for calibration.…”

Section: Fviii/vwf Complex Purificationmentioning

confidence: 99%

Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

Santizo

Zenteno

Pina-Canseco

et al. 2009

Tohoku J. Exp. Med.

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The human coagulation factor VIII (FVIII) is an essential cofactor for the proteolytic activation of factor X. FVIII is activated by thrombin and blood coagulation factor Xa; factor IXa (FIXa) activates factor X (FXa), requiring Ca 2+ , phospholipids, and activated Factor VIII (FVIIIa) (Schmidt et al. 2005). FVIII and von Willebrand factor (VWF) form a non-covalently bound complex. This complex (FVIII/ VWF) circulates in the human plasma, is critical to homeostasis, and normally exists in inactive form. The binding of FVIII to VWF is essential for the survival of FVIII in vivo (Kaufman and Pipe 1999). Deficiencies or structural defects in FVIII are responsible for the most common inherited bleeding disorders, such as hemophilia and von Willebrand disease (Lillicrap 2008).FVIII is a polypeptide of 2332 amino acids, synthesized in the liver by parenchyma cells and hepatic sinusoidal endothelium cells, as well as by the pulmonary endothelium. FVIII has several glycosylation sites that appear to be important in its circulation kinetics. This factor possesses N-glycosydically linked glycans, which are characterized by a N-acetyl-glucosamine (GlcNAc)-asparagine inner core and are relevant for the folding and productive secretion of FVIII, and O-glycosydically glycans, which are characterized by N-acetyl-galactosamine (GalNAc)-serine/threonine and are involved in determining protein conformation and interact with other glycoproteins. FVIII possesses two unusual mannosylated sites that can be recognized by mannose receptors on Kupffer cells (Dasgupta et al. 2007).

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Standardization of the One-stage Assay for Factor VIII (Antihemophilic Factor)

Cited by 25 publications

References 14 publications

Proficiency Testing of Factor VIII:C Activitiy Assays at the Canadian Red Cross Society National Reference Laboratory

Proficiency Testing of Factor VIII:C Activitiy Assays at the Canadian Red Cross Society National Reference Laboratory

The therapeutic effect of bone marrow–derived liver cells in the phenotypic correction of murine hemophilia A

Lectin Activity of the Coagulation Factor VIII/von Willebrand Complex

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