-transparent.png){kind=logo}
Blood coagulation factor VII is a vitamin K dependent glycoprotein which in its activated form, factor VIIa, participates in the coagulation process by activating factor X and/or factor IX in the presence of Ca2+ and tissue factor. Three types of potential posttranslational modifications exist in the human factor VIIa molecule, namely, 10 gamma-carboxylated, N-terminally located glutamic acid residues, 1 beta-hydroxylated aspartic acid residue, and 2 N-glycosylated asparagine residues. In the present study, the amino acid sequence and posttranslational modifications of recombinant factor VIIa as purified from the culture medium of a transfected baby hamster kidney cell line have been compared to human plasma factor VIIa. By use of HPLC, amino acid analysis, peptide mapping, and automated Edman degradations, the protein backbone of recombinant factor VIIa was found to be identical with human factor VIIa. Neither recombinant factor VIIa nor human plasma factor VIIa was found to contain beta-hydroxyaspartic acid. In human plasma factor VIIa, the 10 N-terminally located glutamic acid residues were found to be fully gamma-carboxylated whereas 9 full and 1 partial gamma-carboxylated residues were found in the corresponding positions of the recombinant factor VIIa molecule. Asparagine residues 145 and 322 were found to be fully N-glycosylated in human plasma factor VIIa. In the recombinant factor VIIa, asparagine residue 322 was fully glycosylated whereas asparagine residue 145 was only partially (approximately 66%) glycosylated. Besides minor differences in the sialic acid and fucose contents, the overall carbohydrate compositions were nearly identical in recombinant factor VIIa and human plasma factor VIIa.(ABSTRACT TRUNCATED AT 250 WORDS)
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
January 1991,
The Biochemical journal,
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
August 1993,
Biochemical and biophysical research communications,
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
August 1988,
The EMBO journal,
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
December 1966,
The Biochemical journal,
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
January 1970,
Acta pathologica et microbiologica Scandinavica. Section B: Microbiology and immunology,
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
April 1992,
The Journal of biological chemistry,
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
January 1991,
Protein expression and purification,
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
June 1991,
The Biochemical journal,
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
August 1988,
Biochemistry,
L Thim, and
S Bjoern, and
M Christensen, and
E M Nicolaisen, and
T Lund-Hansen, and
A H Pedersen, and
U Hedner
January 2010,
Methods in molecular biology (Clifton, N.J.),
