Effect of Ca2+ on the structure and function of factor VIIa.
Binding of Ca2+ to factor VIIa is required for its binding to phospholipids, tissue factor, and for obtaining full amidolytic activity. This presentation describes various binding studies performed with recombinant factor VIIa and fragments hereof in order to localize Ca2+ sites and obtain a better understanding of the functional implication of Ca2+ binding to these sites. Results obtained by means of Ca2+-dependent monoclonal antibodies, immunosorbent assays, intrinsic protein fluorescence and terbium luminescence technique are described and the results are interpreted in terms of a putative model.
Vessel Wall Biology, Health Care Discovery, Novo Nordisk A/S, Gentofte, Denmark.
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Petersen
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Persson
D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000502:physiology; D015942:Factor VIIa / Q000737:chemistry* / Q000502:physiology; D005453:Fluorescence; D007163:Immunosorbent Techniques; D010750:Phosphoproteins / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D013329:Structure-Activity Relationship; D013925:Thromboplastin / Q000737:chemistry
D002135:Calcium-Binding Proteins; D010750:Phosphoproteins; D011994:Recombinant Proteins; D013925:Thromboplastin; D015942:Factor VIIa