1999
DOI: 10.1046/j.1432-1327.1999.00258.x
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Abstract: Activation of the zymogen factor VII yields an enzyme form, factor VIIa, with only modest activity. The thermal effect on this low activity of factor VIIa and its enhancement by the cofactor tissue factor was investigated. Factor VIIa activity measured with a chromogenic peptide substrate is characterized by an unusual temperature dependency which indicates that the activated protease exists in an equilibrium between a latent (enzymatically inactive) and an active conformation. As shown by calorimetry and acti… Show more

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Cited by 11 publications
(6 citation statements)
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“…The accessibility of the N-terminal ␣-amino group of the protease domain of FVIIa has been shown to be inf luenced by TF binding (8), active site occupancy (9), and temperature (28). These observations suggest that the accessibility appears to be an inverse ref lection of the activity state of wild-type FVIIa, with a less accessible N terminus in the active FVIIa conformation.…”
Section: Inhibition Of Fviia Mutants By Atmentioning
confidence: 99%
“…The accessibility of the N-terminal ␣-amino group of the protease domain of FVIIa has been shown to be inf luenced by TF binding (8), active site occupancy (9), and temperature (28). These observations suggest that the accessibility appears to be an inverse ref lection of the activity state of wild-type FVIIa, with a less accessible N terminus in the active FVIIa conformation.…”
Section: Inhibition Of Fviia Mutants By Atmentioning
confidence: 99%
“…The extended contact area restricts the segmental flexibility of FVIIa and positions the active site at an appropriate distance above the membrane surface () for cleavage of the physiological substrates factors IX and X (FX). Moreover, free FVIIa is a modestly active enzyme, but upon binding to TF the active conformation of the serine protease domain is stabilized as manifested by the insertion of the N-terminus into the body of the domain ( , ). A structural change in the N-terminal region upon activation and TF binding has also been demonstrated using a monoclonal antibody ().…”
mentioning
confidence: 99%
“…The PT is the overall result of several sequential enzyme reactions. The effect of temperature on the velocity of enzyme reactions may be due to several different causes, eg an effect on the stability of the enzyme, an effect on the enzyme reaction itself or conformational changes 10,11 . The PT is influenced by several plasma coagulation factors, ie Factors I, II, V, VII, X and by the tissue factor.…”
Section: Discussionmentioning
confidence: 99%
“…The effect of temperature on the velocity of enzyme reactions may be due to several different causes, eg an effect on the stability of the enzyme, an effect on the enzyme reaction itself or conformational changes. 10 , 11 The PT is influenced by several plasma coagulation factors, ie Factors I, II, V, VII, X and by the tissue factor. At present, it is not possible to derive a theoretical model describing the temperature dependence of a complex enzymatic system as the PT.…”
Section: Discussionmentioning
confidence: 99%