tailieunhanh - Báo cáo Y học: Interaction of bovine coagulation factor X and its glutamic-acid-containing fragments with phospholipid membranes A surface plasmon resonance study

The interaction of blood coagulation factor X and its Gla-containing fragments with negatively charged phospholipid membranes composed of 25 mol% phosphatidylserine (PtdSer) and 75 mol% phosphatidylcholine (PtdCho) was studied by surface plasmon resonance. The binding to 100 mol% PtdCho membranes was negligible. The calcium dependence in the membrane binding was evaluated for intact bovine factor X (factor X) and the fragment containing the Gla-domain and the N-terminal EGF (epidermal growth factor)-like domain, Gla–EGFN, from factor X | Eur. J. Biochem. 269 3041-3046 2002 FEBS 2002 doi Interaction of bovine coagulation factor X and its glutamic-acid-containing fragments with phospholipid membranes A surface plasmon resonance study Eva-Maria Erb1 Johan Stenflo1 and Torbjorn Drakenberg2 1 Department of Clinical Chemistry University Hospital Malmo Lund University Malmo Sweden 2Department of Biophysical Chemistry Lund University Lund Sweden The interaction of blood coagulation factor X and its Gla-containing fragments with negatively charged phospholipid membranes composed of 25 mol phosphatidylserine PtdSer and 75 mol phosphatidylcholine PtdCho was studied by surface plasmon resonance. The binding to -00 mol PtdCho membranes was negligible. The calcium dependence in the membrane binding was evaluated for intact bovine factor X factor X and the fragment containing the Gla-domain and the N-terminal EGF epidermal growth factor -like domain Gla-EGFN from factor X. Both proteins show the same calcium dependence in the membrane binding. Calcium binding is cooperative and halfmaximum binding was observed at mM and mM with the best fit to the experimental data with three cooperatively bound calcium ions for both the intact protein and the fragment. The dissociation constant Kd for binding to membranes containing 25 mol PtdSer decreased from M for the isolated Gla-domain to - M for the fragments Gla-EGFN and Gla-EGFNC the Gla-domain and both EGF-like domains fragments and to 40 nM for the entire protein as zymogen activated enzyme or in the activesite inhibited form. Analysis of the kinetics of adsorption and desorption confirmed the equilibrium binding data. Keywords blood coagulation membrane binding calcium dependence factor X Gla-domain. Blood coagulation factor X belongs to the family of vitamin K-dependent proteins. It consists of an NH2-terminal y-carboxyglutamic acid Gla -containing domain followed by two epidermal growth factor EGF -like domains and a .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• medical research
• hemoglobin
• medical knowledge
• medical textbooks
• medical practice
• specialized medicine
• Encyclopedia of Medical Anthropology
• medical
• health
• medical term dictionary
• y tế
• sức khỏe
• Data Mining and Medical Knowledge Management
• Premier Reference Sourse
• statements and documents scientific reports
• medical reports
• medical transfer
• the developing countries
• clinical trials
• medical management
• health care
• Healthcare knowledge management
• Knowledge identification
• Know How and Knowing That cartography
• Knowledge visualization
• Improving knowledge management
• Knowledge workers’ identities
• Evidence from the medical profession
• Knowledge workers
• Medical profession
• Organizational identification
• Knowledge Management
• Data Mining
• Text Mining
• Mapping Medical
• Bioinformatics Challenges
• Digital Libraries
• Medical Informatics
• A Handbook for Medical Teachers
• Medical Teachers
• health education
• health knowledge