scholarly journals Purification and characterization of a highly purified human factor VIII consisting of a single type of polypeptide chain.

1982 ◽  
Vol 79 (23) ◽  
pp. 7200-7204 ◽  
Author(s):  
P. J. Fay ◽  
S. I. Chavin ◽  
D. Schroeder ◽  
F. E. Young ◽  
V. J. Marder
Keyword(s):  
Factor Viii ◽  
Human Factor ◽  
Polypeptide Chain ◽  
Single Type ◽  
Purification And Characterization ◽  
Human Factor Viii

scholarly journals Human factor VIII from heparinized plasma. Purification and characterization of a single-chain form

1988 ◽  
Vol 170 (3) ◽  
pp. 521-528 ◽  
Author(s):  
Peter R. GANZ ◽  
Eilleen S. TACKABERRY ◽  
Douglas S. PALMER ◽  
Gail ROCK
Keyword(s):  
Factor Viii ◽  
Human Factor ◽  
Single Chain ◽  
Purification And Characterization ◽  
Human Factor Viii ◽  
Chain Form

scholarly journals Studies on the purification and characterization of human factor VIII

1972 ◽  
Vol 51 (8) ◽  
pp. 2151-2161 ◽  
Author(s):  
Sally L. Marchesi ◽  
N. Raphael Shulman ◽  
Harvey R. Gralnick
Keyword(s):  
Factor Viii ◽  
Human Factor ◽  
Purification And Characterization ◽  
Human Factor Viii

scholarly journals Characterization of human factor VIII and interaction with von Willebrand factor. An electron microscopic study

1990 ◽  
Vol 194 (2) ◽  
pp. 491-498 ◽  
Author(s):  
Harry F. G. HEIJNEN ◽  
Joost. A. KOEDAM ◽  
Helena SANDBERG ◽  
Nel H. BEESER-VISSER ◽  
Jan. W. SLOT ◽  
...  
Keyword(s):  
Factor Viii ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Von Willebrand Factor ◽  
Human Factor ◽  
Electron Microscopic ◽  
Human Factor Viii ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Studies of the human factor VIII/von Willebrand's factor protein. II. Identification and characterization of the von Willebrand protein

Blood ◽  
1975 ◽  
Vol 46 (3) ◽  
pp. 417-430
Author(s):  
HR Gralnick ◽  
BS Coller
Keyword(s):  
Factor Viii ◽  
Human Factor ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Related Protein ◽  
Human Factor Viii ◽  
Von Willebrand’S Factor ◽  
Von Willebrand ◽  
Identification And Characterization

The purified factor VIII-related protein we have previously characterized from normal cryoprecipitate possesses both procoagulant activity and vWf activity. We have attempted to isolate and characterize this protein from three patients with severe vWd. This protein is absent or markedly diminished in amount in these vWd patients, as judged by gel filtration, polyacrylamide-gel electrophoresis, and immunoprecipitation assays. Likewise, the procoagulant and vWf activities are deficient. As vWf activity is one of the major biologic functions of either the normal or hemophilic factor VIII-related protein, the purified protein should be designated the f VIII/vWf protein.

Characterization of a nondeleterious L1 insertion in an intron of the human factor VIII gene and further evidence of open reading frames in functional L1 elements

Genomics ◽  
1989 ◽  
Vol 4 (3) ◽  
pp. 290-296 ◽  
Author(s):  
Patricia Woods-Samuels ◽  
Corinne Wong ◽  
Stephen L. Mathias ◽  
Alan F. Scott ◽  
Haig H. Kazazian ◽  
...  
Keyword(s):  
Factor Viii ◽  
Human Factor ◽  
Open Reading Frames ◽  
Factor Viii Gene ◽  
Human Factor Viii ◽  
Reading Frames

Affinity Purification of Plasma Proteins: Characterization of Six Affinity Matrices and their Application for the Isolation of Human Factor VIII

1989 ◽  
Vol 61 (02) ◽  
pp. 234-237 ◽  
Author(s):  
M P W M te Booy ◽  
W Riethors ◽  
A Faber ◽  
J Over ◽  
B W König
Keyword(s):  
Factor Viii ◽  
Immunoglobulin G ◽  
Plasma Proteins ◽  
Human Factor ◽  
Specific Activity ◽  
Affinity Purification ◽  
Coagulation Factor ◽  
Affinity Matrix ◽  
Human Factor Viii

SummaryFor the purification of coagulation factor VIII, (1,1’-carbonyldiimida zole [CDI] -activated) Sepharose CL-48 was functionalized with two aminoalkyl and four aminoalkyl-carbamylalkyl ligand- spacer combinations. The affinity matrices were contacted with human plasma. All affinity matrices showed complete adsorption of factor VIII (>90%) and three aminoalkyl-carbamylalkyl Sepharoses gave factor-VIII recoveries of 50-65% and a factor-VIII preparation with a specific activity of 1–2 U factor VIII/mg of protein. Furthermore, no fibrinogen, immunoglobulin G and albumin could be detected in the isolated factor VIII. Optimal results were obtained using the di-methyl-aminopropyl-carbamylpentyl-Sepharose affinity matrix.

scholarly journals Isolation and characterization of thrombin-activated human factor VIII.

1994 ◽  
Vol 269 (8) ◽  
pp. 6246-6251
Author(s):  
J.E. Curtis ◽  
S.L. Helgerson ◽  
E.T. Parker ◽  
P. Lollar
Keyword(s):  
Factor Viii ◽  
Human Factor ◽  
Isolation And Characterization ◽  
Human Factor Viii

scholarly journals Isolation and Characterization of Human Factor VIII (Antihemophilic Factor)

1973 ◽  
Vol 248 (11) ◽  
pp. 3946-3955 ◽  
Author(s):  
Mark E. Legaz ◽  
Gottfried Schmer ◽  
Richard B. Counts ◽  
Earl W. Davie
Keyword(s):  
Factor Viii ◽  
Human Factor ◽  
Isolation And Characterization ◽  
Human Factor Viii ◽  
Antihemophilic Factor

scholarly journals Studies of the human factor VIII/von Willebrand's factor protein. II. Identification and characterization of the von Willebrand protein

Blood ◽  
1975 ◽  
Vol 46 (3) ◽  
pp. 417-430 ◽  
Author(s):  
HR Gralnick ◽  
BS Coller
Keyword(s):  
Factor Viii ◽  
Human Factor ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Related Protein ◽  
Human Factor Viii ◽  
Von Willebrand’S Factor ◽  
Von Willebrand ◽  
Identification And Characterization

Abstract The purified factor VIII-related protein we have previously characterized from normal cryoprecipitate possesses both procoagulant activity and vWf activity. We have attempted to isolate and characterize this protein from three patients with severe vWd. This protein is absent or markedly diminished in amount in these vWd patients, as judged by gel filtration, polyacrylamide-gel electrophoresis, and immunoprecipitation assays. Likewise, the procoagulant and vWf activities are deficient. As vWf activity is one of the major biologic functions of either the normal or hemophilic factor VIII-related protein, the purified protein should be designated the f VIII/vWf protein.

Sign in / Sign up

Export Citation Format

Share Document