1995
DOI: 10.1111/j.1432-1033.1995.293_c.x
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Abstract: The structural and functional effects of Ca'+ binding to vitamin-K-dependent coagulation factor VIIa were investigated. Conformational changes with a midpoint around 0.7 mM Ca2+ quenched the intrinsic protein fluorescence of a fragment of factor VIIa comprising only the light chain and this coincided with an increase in factor VIIa amidolytic activity in the absence of tissue factor. Ca'+ binding to sites in factor VIIa and in the fragment with an apparent dissociation constant of 1.3 -1.4 mM induced binding t… Show more

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Cited by 32 publications
(48 citation statements)
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References 47 publications
(30 reference statements)
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“…A lower apparent binding of F6A4 was observed for 735V-fVIIa. Residue 35 is either part of or in close proximity of the epitope [14] and the lower response supports the assumption that the T35V mutation introduces structural changes that also may cause the decreased TF binding, The Ca 2+ dependencies of all fVIIa mutants for binding to F6A4 were nevertheless similar to that of the wild-type protein (Fig. 2).…”
Section: Resultssupporting
confidence: 66%
See 1 more Smart Citation
“…A lower apparent binding of F6A4 was observed for 735V-fVIIa. Residue 35 is either part of or in close proximity of the epitope [14] and the lower response supports the assumption that the T35V mutation introduces structural changes that also may cause the decreased TF binding, The Ca 2+ dependencies of all fVIIa mutants for binding to F6A4 were nevertheless similar to that of the wild-type protein (Fig. 2).…”
Section: Resultssupporting
confidence: 66%
“…The two forms were identified by mass spectrometry and N-terminal amino acid sequencing (with positive identification of Gla) of peptic and tryptic peptides (manuscript in preparation). The ELISA employing the monoclonal antibodies F1A2 and F6A4 was carried out as described [14]. SDS-PAGE was run according to Laemmli [15].…”
Section: Proteins Materials and Standard Methodsmentioning
confidence: 99%
“…Removal of Ca 2ϩ reduces the activity of FVIIa to less than 10% (14), indicating the potentially essential charge-neutraliz- (43,44). FIXa is also modestly stimulated (3-fold), and this has, like for FVIIa, been shown to be accompanied by insertion of the N terminus into the activation pocket (45) , and Met 298 play significant roles in, but are not fully responsible for, maintaining this physiological control mechanism.…”
Section: Discussionmentioning
confidence: 99%
“…Upon binding of the cofactors, an activity increase of several 1,000-fold is observed, in part by shifting the equilibrium from the zymogen-like form toward the catalytically active conformation of FVIIa (12,13). Ca 2ϩ binding alone leads to a more than 10-fold increase in activity (14).…”
Section: ؉mentioning
confidence: 99%
“…It is the light chain of FVII that contains the first epidermal growth factor-like domain (EGF-1), a stretch of 37 amino acids with characteristic structure that has been implicated as the principal site of FVII interaction with TF (5)(6)(7)(8). The FVII molecule also requires calcium for the expression of optimum activity, one molecule of which is bound in each of the protease domains (9,10) and the EGF-1 domain at a high affinity site (11), with seven more Ca 2ϩ molecules bound with variable affinity by the Gla domain (12).…”
mentioning
confidence: 99%