Plasma Fractions Rich in Factor VIII

2015 ◽  
pp. 1094-1099
Author(s):  
E. Deutsch ◽  
M. Fischer
Keyword(s):  
Factor Viii ◽  
Plasma Fractions

Human Plasma and Plasma Fractions as Sources of Factor VIII (Antihaemophilic Factor)

Vox Sanguinis ◽  
1969 ◽  
Vol 16 (4-5) ◽  
pp. 382-397
Author(s):  
M. Verstraete ◽  
P. Olislaegers ◽  
H. van Itterbeek ◽  
P. Waumans ◽  
A. Lust
Keyword(s):  
Factor Viii ◽  
Human Plasma ◽  
Plasma Fractions

scholarly journals The Apparent Separation of Factor VIII Related Antigen and Coagulant Activity from von Willebrand Factor Activity by an Immunoadsorbent

1977 ◽  
Author(s):  
H. A. Cooper ◽  
D. Lee ◽  
M. A. Lamb ◽  
R. H. Wagner
Keyword(s):  
Factor Viii ◽  
Human Plasma ◽  
Human Factor ◽  
Solid Phase ◽  
Residual Activity ◽  
Normal Human Plasma ◽  
Human Factor Viii ◽  
Coagulant Activity ◽  
Plasma Fractions ◽  
Normal Human

An antibody was raised in rabbits to the small active fragment of human factor VIII. The antigen was obtained by Ca2+ dissociation of a human factor VIII preparation made from a multidonor pool of plasma. After two adsorptions with 0.1 volume of normal human plasma, the antibody neutralized the F. VIII coagulant activity of normal human plasma, but did not precipitate with any plasma or plasma fractions nor did it neutralize vWF activity as measured by ristocetin aggregation of fixed washed platelets. A solid phase immunochemical reagent was prepared by CNBr binding of the partially purified rabbit antibody to 1% agarose beads. Non-immune beads were similarly prepared with IgG fractions from a normal non-immunized rabbit. Using a batch technique the beads were studied for their ability to remove F. VIII coagulant, F. VIII Ag, and vWF activity from normal human plasma. Assay of the supernatant plasma after 2 hrs, 22°, from 10 replicate experiments gave the following results for residual activity, as per cent of non-immune bead control:F. VIII (37.5±4), F. VIII-Ag (30.8±9.7), and vWF (72.1±16). The experiment was repeated with 6 replicate samples with higher ratio of beads to plasma with essentially similar results. This unexpected separation of F. VIII-Ag from vWF activity prompted further investigation into how these activities are related to the molecular structure of F. VIII and vWF.

Human Plasma and Plasma Fractions as Sources of Factor VIII (Antihaemophilic Factor)

Vox Sanguinis ◽  
1969 ◽  
Vol 16 (5) ◽  
pp. 382-397 ◽  
Author(s):  
M. Verstraete ◽  
P. Olislaegers ◽  
H. Itterbeek ◽  
P. Waumans ◽  
A. Lust
Keyword(s):  
Factor Viii ◽  
Human Plasma ◽  
Plasma Fractions

Human Plasma and Plasma Fractions as Sources of Factor VIII (Antihaemophilic Factor)

2015 ◽  
pp. 382-397
Author(s):  
M. Verstraete ◽  
P. Olislaegers ◽  
H. van Itterbeek ◽  
P. Waumans ◽  
A. Lust
Keyword(s):  
Factor Viii ◽  
Human Plasma ◽  
Plasma Fractions

scholarly journals Different Forms of Factor VIII Related Antigens in Endothelial Cell Cultures, Cryoprecipitate Supernatant and Normal Plasma

1977 ◽  
Author(s):  
I. R. Peake ◽  
A. L. Bloom ◽  
S. A. M. Shearn
Keyword(s):  
Endothelial Cell ◽  
Factor Viii ◽  
Cell Cultures ◽  
Gel Filtration ◽  
Rabbit Antiserum ◽  
Response Curves ◽  
Normal Plasma ◽  
Plasma Fractions ◽  
Endothelial Cell Cultures ◽  
Antigenic Reactivity

The nature of factor VIII related antigen (FVIIIRAG) was studied in endothelial cell cultures (EC), cryoprecipitate supernatant (cryo-S) and gel-filtered plasma fractions (GPF). Antigenic reactivity (AR) was assessed using the Laurell electroimmunoassay (LA) and a two-site immunoradiometric assay (IRMA) using a non-coagulation inhibitory rabbit antiserum raised against a factor VIII concentrate prepared by cryoprecipitation and gel filtration. Electrophoretic mobility (EM) of FVIIIRAG was assessed by two dimensional crossed immunoelectrophoresis (2DCIE), ristocetin co-factor activity (RiCoF) was estimated using fixed platelets. In normal plasma the results of LA, RiCoF assay and IRMA were in agreement. FVIIIRAG synthesised by EC showed increased EM and, in the IRMA decreased AR when compared to LA often with non-parallel dose response curves (DRC). This effect was not prevented by the presence of protease inhibitors in the culture medium. RiCoF activity was reduced compared with. LA and was related to the parallelism of the DRC in the IRMA. In cryo-S and the late eluting GPFs increased EM of FVIIIRAG was seen, and in these preparations also the DRC of the IRMA were not parallel to the normal plasma DRC. AR and RiCoF activity were disproportionately reduced when compared to the LA. It is concluded that the IRMA is sensitive to the presence of different forms of FVIIIRAG, particularly those which exhibit low levels of RiCoF activity and increased EM. some of these forms are present in normal plasma.

The diagnosis and management of factor VIII and IX inhibitors: a guideline from the UK Haemophilia Centre Doctors' Organization (UKHCDO)

2000 ◽  
Vol 111 (1) ◽  
pp. 78-90 ◽  
Author(s):  
C. R. M. Hay ◽  
T. P. Baglin ◽  
P. W. Collins ◽  
F. G. H. Hill ◽  
D. M. Keeling
Keyword(s):  
Factor Viii ◽  
Diagnosis And Management ◽  
Viii And Ix ◽  
The Uk

Purity of factor VIII product and incidence of inhibitors in previously untreated patients with haemophilia A

Haemophilia ◽  
2001 ◽  
Vol 7 (4) ◽  
pp. 364-368 ◽  
Author(s):  
E. P. Mauser-Bunschoten ◽  
J. G. Van Der Bom ◽  
M. Bongers ◽  
M. Twijnstra ◽  
G. Roosendaal ◽  
...  
Keyword(s):  
Factor Viii ◽  
Haemophilia A ◽  
Viii Product
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