Search results for: Magdalena Svensson

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article

Effects on the conformation of FVIIa by sTF and Ca2+ binding: Studies of fluorescence resonance energy transfer and quenching

Karin Carlsson, Egon Persson, Mikael Lindgren, Uno Carlsson, more

Biochemical and Biophysical Research Communications > 2011 > 413 > 4 > 545-549

The apparent length of FVIIa in solution was estimated by a FRET analysis. Two fluorescent probes, fluorescein (Fl-FPR) and a rhodamine derivative (TMR), were covalently attached to FVIIa. The binding site of Fl-FPR was in the protease domain whereas TMR was positioned in the Gla domain, thus allowing a length measure over virtually the whole extension of the protein. From the FRET measurements, the...

article

Inhibitors of factor VIIa affect the interface between the protease domain and tissue factor

Karin Carlsson, Egon Persson, Uno Carlsson, Magdalena Svensson

Biochemical and Biophysical Research Communications > 2006 > 349 > 3 > 1111-1116

Blood coagulation is triggered by the formation of a complex between factor VIIa (FVIIa) and its cofactor, tissue factor (TF). The γ–carboxyglutamic acid-rich domain of FVIIa docks with the C-terminal domain of TF, the EGF1 domain of FVIIa contacts both domains of TF, and the EGF2 domain and protease domain (PD) form a continuous surface that sits on the N-terminal domain of TF. Our aim was to investigate...

article

Sequential coagulation factor VIIa domain binding to tissue factor

Maria Österlund, Egon Persson, Uno Carlsson, Per-Ola Freskgård, more

Biochemical and Biophysical Research Communications > 2005 > 337 > 4 > 1276-1282

Vessel wall tissue factor (TF) is exposed to blood upon vascular damage which enables association with factor VIIa (FVIIa). This leads to initiation of the blood coagulation cascade through localization and allosteric induction of FVIIa procoagulant activity. To examine the docking pathway of the FVIIa–TF complex, various residues in the extracellular part of TF (sTF) that are known to interact with...

article

Activity, Folding, Misfolding, and Aggregation in Vitro of the Naturally Occurring Human Tissue Factor Mutant R200W ^†

Jimmy Wiréhn, Karin Carlsson, Anna Herland, Egon Persson, more

Biochemistry > 2005 > 44 > 18 > 6755 - 6763

article

Transition state analysis of the complex between coagulation factor VIIa and tissue factor: suggesting a sequential domain-binding pathway

Maria Österlund, Egon Persson, Magdalena Svensson, Uno Carlsson, more

Biochemical and Biophysical Research Communications > 2005 > 327 > 3 > 789-793

Injury of a blood vessel exposes membrane-bound tissue factor (TF) to blood, which allows binding of coagulation factor VIIa (FVIIa). This initiation of the coagulation cascade is dictated by a specific multi-domain interaction between FVIIa and TF. To examine the energies involved in the transition state of the FVIIa:TF complex, various residues in the extracellular part of TF (sTF) that are known...

article

Site-directed fluorescence probing to dissect the calcium-dependent association between soluble tissue factor and factor VIIa domains

Karin Carlsson, Maria Österlund, Egon Persson, Per-Ola Freskgård, more

BBA - Proteins and Proteomics > 2003 > 1648 > 1-2 > 12-16

We have used the site-directed labeling approach to study the Ca ² ⁺ -dependent docking of factor VIIa (FVIIa) to soluble tissue factor (sTF). Nine Ca ² ⁺ binding sites are located in FVIIa and even though their contribution to the overall binding between TF and FVIIa has been thoroughly studied, their importance for local protein-protein interactions within the complex has...

article

Spin and Fluorescent Probing of the Binding Interface between Tissue Factor and Factor VIIa at Multiple Sites

Rikard Owenius, Maria Österlund, Magdalena Svensson, Mikael Lindgren, more

Biophysical Journal > 2001 > 81 > 4 > 2357-2369

The specific complex between the extracellular part of tissue factor (sTF) and factor VIIa (FVIIa) was chosen as a model for studies of the binding interface between two interacting proteins. Six surface-exposed positions in sTF, residues known to contribute to the sTF-FVIIa interaction, were selected for cysteine mutation and site-directed labeling with spin and fluorescent probes. The binding interface...

article

Probing Inhibitor-Induced Conformational Changes along the Interface between Tissue Factor and Factor VIIa

Maria Österlund, Rikard Owenius, Karin Carlsson, Uno Carlsson, more

Biochemistry > 2001 > 40 > 31 > 9324 - 9328

article

Properties of Spin and Fluorescent Labels at a Receptor-Ligand Interface

Rikard Owenius, Maria Österlund, Mikael Lindgren, Magdalena Svensson, more

Biophysical Journal > 1999 > 77 > 4 > 2237-2250

Site-directed labeling was used to obtain local information on the binding interface in a receptor-ligand complex. As a model we have chosen the specific association of the extracellular part of tissue factor (sTF) and factor VIIa (FVIIa), the primary initiator of the blood coagulation cascade. Different spectroscopic labels were covalently attached to an engineered cysteine in position 140 in sTF,...

article

Cis-trans isomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase

Cecilia Fransson, Per-Ola Freskgård, Helena Herbertsson, Åsa Johansson, more

FEBS Letters > 1992 > 296 > 1 > 90-94

The refolding of human carbonic anhydrase II is a sequential process. The slowest step involved is the recovery of enzymic activity (t ₁ ₂ =9 min). Kinetic data from 'double-jump' measurements indicate that proline isomerization might be rate determining, in the reactivation of the denatured enzyme. Proof of this is provided by the effect of proline isomerase on the reactivation kinetics;...

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