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

Investigations on the Nature of Hemophilia A

1963 ◽  
Vol 09 (01) ◽  
pp. 030-052 ◽  
Author(s):  
Eberhard Mammen
Keyword(s):  
Factor Viii ◽  
Human Plasma ◽  
Barium Sulfate ◽  
Freeze Drying ◽  
Room Temperature ◽  
Hemophilia A ◽  
Normal Human Plasma ◽  
Normal Human ◽  
And Storage ◽  
Prothrombin Activation

SummaryIn this paper an inhibitor is described that is found in hemophilic plasma and serum different from any till now described inhibitor. The inhibitor only inhibits prothrombin activation in the “intrinsic clotting systems”. This inhibitor is probably not present in normal human plasma or serum. It is destroyed by ether and freeze drying, is labile to acid and storage at room temperature. It is stable upon dialysis and has not been adsorbed on barium sulfate, aluminum hydroxide or kaolin. It precipitates at 50% v/v saturation with alcohol. The nature of this inhibitor seems to be a protein or lipoprotein.Factor VIII was isolated from hemophilic plasma. The amount isolated was the same as from normal plasma and the activity properties were not different. Hemophiliacs have normal amounts of factor VIII.

REACTIONS OF CISPLATIN WITH HUMAN PLASMA AND PLASMA FRACTIONS

Cisplatin ◽  
1980 ◽  
pp. 285-304 ◽  
Author(s):  
Arnold J. Repta ◽  
David F. Long
Keyword(s):  
Human Plasma ◽  
Plasma Fractions

scholarly journals Direct radioimmune detection in human plasma of the association between factor VIII procoagulant protein and von Willebrand factor, and the interaction of von Willebrand factor-bound procoagulant VIII with platelets

Blood ◽  
1983 ◽  
Vol 61 (6) ◽  
pp. 1163-1173 ◽  
Author(s):  
JL Moake ◽  
MJ Weinstein ◽  
JH Troll ◽  
LE Chute ◽  
NM Colannino
Keyword(s):  
Factor Viii ◽  
Human Plasma ◽  
Von Willebrand Factor ◽  
Sodium Dodecylsulfate ◽  
Coagulation Factors ◽  
Cysteine Protease Inhibitors ◽  
Proteolytic Activation ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract The predominant procoagulant factor VIII (VIII:C) form in normal human plasma containing various combinations of anticoagulants and serine/cysteine protease inhibitors is a protein with mol wt 2.6 +/- 0.2 X 10(5). This protein can be detected by 125I-anti-VIII:C Fab binding and gel electrophoresis in the presence and absence of sodium dodecylsulfate (SDS) and is distinct from the subunit of factor VIII/von Willebrand factor (VIII:vWF) multimers. No larger VIII:C form is present in plasma from patients with severe congenital deficiencies of each of the coagulation factors, other than VIII:C. The mol wt approximately 2.6 X 10(5) VIII:C form is, therefore, likely to be the in vivo procoagulant form of VIII:C, rather than a partially proteolyzed, partially activated derivative of a larger precursor. About 60% of this procoagulant mol wt approximately 2.6 X 10(5) VIII:C form in plasma is present in noncovalent complexes with larger VIII:vWF multimers, which attach reversibly to platelet surfaces in the presence of ristocetin. This VIII:vWF-bound protein of mol wt approximately 2.6 X 10(5) may be the plasma procoagulant form of VIII:C which, after proteolytic activation, accelerates the IXa-mediated cleavage and activation of X postulated to occur on platelet surfaces.

scholarly journals Plasma Lipoprotein Distribution of Liposomal Nystatin Is Influenced by Protein Content of High-Density Lipoproteins

1998 ◽  
Vol 42 (8) ◽  
pp. 1878-1888 ◽  
Author(s):  
Shawn M. Cassidy ◽  
Frank W. Strobel ◽  
Kishor M. Wasan
Keyword(s):  
Human Plasma ◽  
Protein Concentration ◽  
Density Lipoprotein ◽  
High Density ◽  
Plasma Lipoprotein ◽  
High Density Lipoproteins ◽  
Plasma Samples ◽  
Lipoprotein Lipid ◽  
Plasma Fractions ◽  
Lipoprotein Distribution

ABSTRACT The plasma lipoprotein distribution of free nystatin (Nys) and liposomal nystatin (L-Nys) in human plasma samples with various lipoprotein lipid and protein concentrations and compositions was investigated. To assess the lipoprotein distributions of Nys and L-Nys, human plasma was incubated with Nys and L-Nys (equivalent to 20 μg/ml) for 5 min at 37°C. The plasma was subsequently partitioned into its lipoprotein and lipoprotein-deficient plasma fractions by step-gradient ultracentrifugation, and each fraction was analyzed for Nys content by high-pressure liquid chromatography. The lipid and protein contents and compositions of each fraction were determined with enzymatic kits. Following the incubation of Nys and L-Nys in human plasma the majority of Nys recovered within the lipoprotein fractions was recovered from the high-density lipoprotein (HDL) fraction. Incorporation of Nys into liposomes consisting of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol significantly increased the percentage of drug recovered within the HDL fraction. Furthermore, it was observed that as the amount of HDL protein decreased the amounts of Nys and L-Nys recovered within this fraction decreased. These findings suggest that the preferential distribution of Nys and L-Nys into plasma HDL may be a function of the HDL protein concentration.

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