Isolation and characterization of human factor IX cDNA: Identification of Taq I polymorphism and regional assignment

1984 ◽  
Vol 10 (5) ◽  
pp. 465-473 ◽  
Author(s):  
Pudur Jagadeeswaran ◽  
Don E. Lavelle ◽  
Rajinder Kaul ◽  
T. Mohandas ◽  
Stephen T. Warren
Keyword(s):  
Human Factor ◽  
Factor Ix ◽  
Isolation And Characterization ◽  
Human Factor Ix ◽  
Regional Assignment

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 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.

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

Isolation and Characterization of Canine Factor IX

1996 ◽  
Vol 75 (03) ◽  
pp. 450-455 ◽  
Author(s):  
Yuichi Sugahara ◽  
James Catalfamo ◽  
Marjory Brooks ◽  
Eri Hitomi ◽  
S Paul Bajaj ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Factor ◽  
Factor Ix ◽  
Hemophilia B ◽  
Enzyme Linked Immunosorbent Assay ◽  
Amino Terminal ◽  
Isolation And Characterization ◽  
Human Factor Ix ◽  
Plasma Factor ◽  
Canine Plasma

SummaryCanine plasma factor IX was purified to homogeneity by a combination of barium citrate precipitation and three-step column chromatographies of DEAE sepharose, heparin agarose and a monoclonal antifactor IX antibody-linked agarose. Canine factor IX has an apparent molecular size of 61 kDa, which is slightly smaller than that of human factor IX, as determined by denatured polyacrylamide gel electrophoresis. Its amino acid composition, amino-terminal and carboxyterminal amino acid sequences agreed well with those predicted from the reported cDNA. Unlike purified human factor IX, canine factor IX preparation often showed a discrete smaller molecular species (∼50 kDa) which was generated by a specific proteolytic cleavage between Arg310 and Val311. When purified canine factor IX was utilized as a standard for enzyme linked immunosorbent assay, the concentration of canine factor IX in the pooled normal dog plasma was determined to be 5.3 Μg/ml with 11.2% carbohydrate content (or 4.7 Μg/ml for its polypeptide chain moiety). Concentration of plasma factor IX antigen was measured in six severely affected, unrelated hemophilia B dogs. Four had factor IX antigen of less than 1% of the normal, and two had undetectable levels. The latter two had gross molecular abnormalities in their factor IX genes. Three obligate carrier females had variable but proportionately reduced factor IX antigen and factor IX coagulant activity levels. These results provide a quantitative method for measuring canine factor IX antigen which is a prerequisite for studying hemostasis and development of gene transfer approaches in the canine model of hemophilia B.

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