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Literature summary for 3.4.21.21 extracted from

  • Broze, G.J.; Majerus, P.W.
    Purification and properties of human coagulation factor VII (1990), J. Biol. Chem., 255, 1242-1247.
    View publication on PubMed
Search for more literature for 3.4.21.21

Inhibitors

Inhibitors Comment Organism Structure
antithrombin III
-
 Homo sapiens
diisopropylfluorophosphate 15 mM, 60 min, 50% inactivation Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 the zymogen, factor VII, is composed of a single polypeptide chain polypeptide of 48000 Da, with the NH2-terminal sequence Ala-Asn-Ala-Phe-Leu-(gamma-carboxyglutamic acid)-(gamma-carboxyglutamic acid)-Leu-Arg-Pro. It is converted to a two-chain form, factor VIIa, connected by disulfide bonds by the action of factor Xa, in the presence of phospholipids and calcium and by factor XIIa, without additional cofactors Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the zymogen, factor VII, is composed of a single polypeptide chain polypeptide of 48000 Da, with the NH2-terminal sequence Ala-Asn-Ala-Phe-Leu-(gamma-carboxyglutamic acid)-(gamma-carboxyglutamic acid)-Leu-Arg-Pro. It is converted to a two-chain form, factor VIIa, connected by disulfide bonds by the action of factor Xa, in the presence of phospholipids and calcium and by factor XIIa, without additional cofactors Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
factor VII Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
plasma
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Homo sapiens