Immunochemical characterization of a low affinity lysine binding site within plasminogen.
Open Access
- 1 November 1981
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 256 (21) , 10864-10869
- https://doi.org/10.1016/s0021-9258(19)68524-8
Abstract
No abstract availableThis publication has 31 references indexed in Scilit:
- On the Kinetics of the Reaction between Human Antiplasmin and a Low-Molecular-Weight Form of PlasminEuropean Journal of Biochemistry, 1978
- Purification and Characterization of Human Antiplasmin, the Fast-Acting Plasmin Inhibitor in PlasmaEuropean Journal of Biochemistry, 1977
- Primary Structure of the B‐Chain of Human PlasminEuropean Journal of Biochemistry, 1977
- Multiple gene duplication in the evolution of plasminogen. Five regions of sequence homology with the two internally homologous structures in prothrombinFEBS Letters, 1976
- A New Method of Isolation and Some Properties of the Heavy Chain of Human PlasminEuropean Journal of Biochemistry, 1975
- Primary Structure of Peptides Released during Activation of Human Plasminogen by UrokinaseEuropean Journal of Biochemistry, 1973
- Rotational diffusion analysis of the conformational alterations produced in plasminogen by certain antifibrinolytic amino acidsBiochemistry, 1973
- Immunobiology of Fibrinogen. EMERGENCE OF NEOANTIGENIC EXPRESSIONS DURING PHYSIOLOGIC CLEAVAGE IN VITRO AND IN VIVOJournal of Clinical Investigation, 1973
- Plasminogen: Purification from Human Plasma by Affinity ChromatographyScience, 1970
- A Method of Trace Iodination of Proteins for Immunologic StudiesInternational Archives of Allergy and Immunology, 1966