Inhibition of fibrin polymerization by fragment D is affected by calcium, Gly-Pro-Arg and Gly-His-Arg
- 1 January 1983
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 742 (1) , 25-32
- https://doi.org/10.1016/0167-4838(83)90354-0
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Potential role of the Aα chain in the binding of calcium to human fibrinogenBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Recalculation of calcium-binding properties of human and rat fibrin(ogen) and their degradation productsThrombosis Research, 1981
- Influence of Calcium Ion on the Binding of Fibrin Amino Terminal Peptides to FibrinogenScience, 1981
- Measurement of fibrinogen degradation products by a sandwich enzyme immunoassay techniqueClinica Chimica Acta; International Journal of Clinical Chemistry, 1980
- Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differencesBiochemistry, 1980
- The possible physiologic importance of calcium complexes: An opinionClinica Chimica Acta; International Journal of Clinical Chemistry, 1979
- Anticlotting properties of fragments D from human fibrinogen and fibrinEuropean Journal of Clinical Investigation, 1979
- Fibrinopeptide B and Aggregation of FibrinogenScience, 1979
- A two-step fibrinogen–fibrin transition in blood coagulationNature, 1978
- Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments DThrombosis Research, 1977