scholarly journals Characterization of the defect in activation of factor IX Chapel Hill by human factor XIa.

1981 ◽  
Vol 68 (6) ◽  
pp. 1420-1426 ◽  
Author(s):  
K M Braunstein ◽  
C M Noyes ◽  
M J Griffith ◽  
R L Lundblad ◽  
H R Roberts
Keyword(s):  
Human Factor ◽  
Factor Ix ◽  
Chapel Hill ◽  
Factor Xia

scholarly journals Expression and characterization of human factor IX. Factor IXthr-397 and factor IXval-397

1991 ◽  
Vol 266 (23) ◽  
pp. 15213-15220
Author(s):  
N. Hamaguchi ◽  
P.S. Charifson ◽  
L.G. Pedersen ◽  
G.D. Brayer ◽  
K.J. Smith ◽  
...  
Keyword(s):  
Human Factor ◽  
Factor Ix ◽  
Human Factor Ix

scholarly journals Purification and characterization of an abnormal factor IX (Christmas factor) molecule. Factor IX Chapel Hill.

1978 ◽  
Vol 62 (5) ◽  
pp. 1078-1085 ◽  
Author(s):  
K S Chung ◽  
D A Madar ◽  
J C Goldsmith ◽  
H S Kingdon ◽  
H R Roberts
Keyword(s):  
Factor Ix ◽  
Purification And Characterization ◽  
Chapel Hill

scholarly journals Construction, Rescue, and Characterization of Vectors Derived from Ovine Atadenovirus

2003 ◽  
Vol 77 (22) ◽  
pp. 11941-11951 ◽  
Author(s):  
Peter Löser ◽  
Christian Hofmann ◽  
Gerald W. Both ◽  
Wolfgang Uckert ◽  
Moritz Hillgenberg
Keyword(s):  
Gene Expression ◽  
Mammalian Cells ◽  
Human Factor ◽  
Insertion Site ◽  
Factor Ix ◽  
Vector System ◽  
Virus Rescue ◽  
Human Factor Ix

ABSTRACT Gene transfer vectors derived from ovine atadenovirus type 7 (OAdV) can efficiently infect a variety of mammalian cells in vitro and in vivo to deliver and express transgenes. However, early OAdV vectors were designed on human mastadenovirus principles prior to the complete characterization of OAdV genes and transcripts. The distinctive arrangement of the OAdV genome has suggested ways to improve OAdV vector design and utility. We therefore developed a cosmid-based approach that allows efficient construction of recombinant ovine atadenovirus genomes in which the transgene is inserted at one of three sites. Viruses were rescued by transfection of viral DNA into a new ovine fetal skin fibroblast producer cell line, HVO156. The suitability of the three insertion sites was compared with respect to virus rescue efficiency, gene expression levels, and genetic stability of the vectors. We found that one vector with a transgene inserted at site 1, between the pVIII and fiber genes, was unstable. Only one vector that carried a transgene at site 2, near the right end of the genome, together with a nearby deletion was rescued. In contrast, several vectors with different transgenes inserted in site 3, between the E4 and RH transcription units, were repeatedly rescued, and these vectors were stable over at least four passages. Transgene orientation in site 3 had only little effect on expression. Finally, a vector carrying a human factor IX cDNA at site 3, when administered intravenously, produced nearly physiological levels of human factor IX in mice. The availability of an efficient method for vector construction and the identification of a new insertion site for virus rescue and gene expression substantially enhance the utility of the OAdV vector system.

scholarly journals Effect of heparin on the inactivation rate of human factor XIa by antithrombin-III

Blood ◽  
1982 ◽  
Vol 60 (4) ◽  
pp. 940-947 ◽  
Author(s):  
CF Scott ◽  
M Schapira ◽  
RW Colman
Keyword(s):  
Clinical Practice ◽  
Human Factor ◽  
Antithrombin Iii ◽  
Fold Increase ◽  
Factor Ix ◽  
Inactivation Rate ◽  
Amidolytic Activity ◽  
Factor Ixa ◽  
Factor Xia ◽  
Plasma Heparin

Abstract Factor XIa catalyzes an important reaction in the early phase of blood coagulation by converting factor IX to an active enzyme (factor IXa). Although antithrombin-III, an inhibitor of factor XIa, normally accounts for only one-sixth of the plasma inhibitory activity against factor XIa, its effectiveness has been reported to be enhanced by heparin. We have reinvestigated the ability of heparin to potentiate factor XIa inhibition by both purified antithrombin-III and plasma using synthetic tripeptide amide substrates as well as a coagulant assay. No increase in the inactivation rate of factor XIa amidolytic activity by purified antithrombin-III was observed in the presence of therapeutic heparin concentrations (1 U/ml), although inhibition of the amidolytic activity of thrombin by purified antithrombin-III was enhanced at least 20-fold by the same concentration of heparin. Furthermore, despite the ability of heparin (1 U/ml) to increase the inactivation rate of thrombin by plasma, no acceleration of the rate of inhibition of factor XIa by plasma was observed. Similar results were found when the inhibition of factor XIa was monitored with a coagulant assay after first removing the heparin. Only at heparin concentrations of 5 and 10 U/ml, was a 2- and 4-fold increase in the inactivation rate of factor XIa by purified antithrombin III observed. Therefore, in both purified systems as well as plasma, heparin, at concentrations observed in clinical practice, does not accelerate the inactivation rate of human factor XIa by antithrombin-III.

scholarly journals Interaction of factor XIa and antithrombin in the presence and absence of heparin

Blood ◽  
1986 ◽  
Vol 67 (5) ◽  
pp. 1488-1492 ◽  
Author(s):  
DL Beeler ◽  
JA Marcum ◽  
S Schiffman ◽  
RD Rosenberg
Keyword(s):  
Protease Inhibitor ◽  
Human Factor ◽  
Sodium Dodecyl ◽  
Factor Ix ◽  
First Order ◽  
Inhibitor Complex ◽  
Sds Page ◽  
Factor Xia ◽  
Presence And Absence ◽  
Antibody Population

Abstract We have studied the interaction between purified human factor XIa and antithrombin in the presence and absence of well-characterized preparations of heparin. The concentrations of hemostatic enzyme, protease inhibitor, and mucopolysaccharide were 5.76 X 10(-8) mol/L, 5.76 X 10(6) mol/L, and either 5.88 X 10(6) mol/L or 0, respectively. Kinetic investigation of this process using a tritiated factor IX substrate demonstrated that the pseudo first-order rate constants of this reaction in the presence and absence of heparin are approximately 1.0 min-1 and approximately 0.025 min-1, respectively. Thus, the rate of hemostatic enzyme-protease inhibitor complex formation is accelerated by about 40-fold in the presence of saturating levels of the mucopolysaccharide. These results were confirmed in a qualitative manner by directly monitoring the generation of factor XIa-antithrombin interaction product with sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis using an antibody population specific for the protease inhibitor.

Characterization of γ-Carboxyglutamic Acid Residue 21 of Human Factor IX†

Biochemistry ◽  
1996 ◽  
Vol 35 (32) ◽  
pp. 10321-10327 ◽  
Author(s):  
Alisa S. Wolberg ◽  
Leping Li ◽  
Wing-Fai Cheung ◽  
Nobuko Hamaguchi ◽  
Lee G. Pedersen ◽  
...  
Keyword(s):  
Human Factor ◽  
Factor Ix ◽  
Human Factor Ix ◽  
Carboxyglutamic Acid

Purification and characterization of human factor IX

1975 ◽  
Vol 7 (3) ◽  
pp. 451-459 ◽  
Author(s):  
L-O. Andersson ◽  
H. Borg ◽  
M. Miller-Andersson
Keyword(s):  
Human Factor ◽  
Factor Ix ◽  
Purification And Characterization ◽  
Human Factor Ix

scholarly journals Expression and characterization of human factor IX and factor IX-factor X chimeras in mouse C127 cells.

1990 ◽  
Vol 265 (1) ◽  
pp. 144-150 ◽  
Author(s):  
S W Lin ◽  
K J Smith ◽  
D Welsch ◽  
D W Stafford
Keyword(s):  
Human Factor ◽  
Factor Ix ◽  
Factor X ◽  
Human Factor Ix
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