Comparison of some properties of native (Glu) and modified (Lys) human plasminogen.
Open Access
- 1 February 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (3) , 733-739
- https://doi.org/10.1016/s0021-9258(17)38164-4
Abstract
No abstract availableThis publication has 29 references indexed in Scilit:
- TREATMENT OF DEEP-VEIN THROMBOSIS WITH INTERMITTENT STREPTOKINASE AND PLASMINOGEN INFUSIONThe Lancet, 1975
- Structural Relationship between "Glutamic Acid" and "Lysine" Forms of Human Plasminogen and Their Interaction with the NH2-Terminal Activation Peptide as Studied by Affinity ChromatographyEuropean Journal of Biochemistry, 1975
- Two distinct pathways of the streptokinase-mediated activation of highly purified human plasminogenBiochemistry, 1974
- Rate of Activation and Electrophoretic Mobility of Unmodified and Partially Degraded Plasminogen Effects of 6-Aminohexanoic Acid and Related CompoundsScandinavian Journal of Clinical and Laboratory Investigation, 1974
- Studies on the Conformational Changes of Plasminogen Induced during Activation to Plasmin and by 6‐Aminohexanoic AcidEuropean Journal of Biochemistry, 1973
- Primary Structure of Peptides Released during Activation of Human Plasminogen by UrokinaseEuropean Journal of Biochemistry, 1973
- Plasminogen: Purification from Human Plasma by Affinity ChromatographyScience, 1970
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- The utilisation of i-dimethylaminonaphthalene-5-sulphonyl chloride for quantitative determination of free amino acids and partial analysis of primary structure of proteinsJournal of Chromatography A, 1970
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965