The Non-covalent interaction between plasmin and α2-antiplasmin
Author:
Publisher
Elsevier BV
Subject
Hematology
Reference25 articles.
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2. Physiological endogenous fibrinolysis: Its congenital abnormalities;Aoki,1983
3. Primary structure of human alpha2-antiplasmin, a serine protease inhibitor (serpin);Holmes;J Biol Chem,1987
4. Amino-acid sequence of human α2-antiplasmin;Lijnen;Eur J Biochem,1987
5. Partial primary structure of human α2-antiplasmin-homology with other plasma protease inhibitors;Lijnen;Thromb Haemost,1982
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2. The interaction between plasminogen and antiplasmin variants as studied by surface plasmon resonance;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2006-11
3. Identification of amino acids in antiplasmin involved in its noncovalent 'lysine-binding-site'-dependent interaction with plasmin;European Journal of Biochemistry;2003-05
4. Lysine-50 is a likely site for anchoring the plasminogen N-terminal peptide to lysine-binding kringles;Protein Science;1998-09
5. Role of the Catalytic Serine in the Interactions of Serine Proteinases with Protein Inhibitors of the Serpin Family;Journal of Biological Chemistry;1995-12
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