A variant of tissue plasminogen activator (t-PA) comprised of the Kringle 2 and the protease domain shows a significant difference in the in vitro rate of plasmin formation as compared to the recombinant human t-PA from transformed chinese hamster ovary cells
- 30 November 1993
- journal article
- Published by Elsevier in Fibrinolysis
- Vol. 7 (6) , 365-372
- https://doi.org/10.1016/0268-9499(93)90060-9
Abstract
No abstract availableThis publication has 7 references indexed in Scilit:
- Binding of fibrin fragments to one-chain and two-chain tissue-type plasminogen activatorBlood, 1992
- Evaluation of thrombolytic and systemic effects of the novel recombinant plasminogen activator BM 06.022 compared with alteplase, anistreplase, streptokinase and urokinase in a canine model of coronary artery thrombosisJournal of the American College of Cardiology, 1992
- Klinische und biochemische Zielsetzungen bei der Thrombolysetherapie mit Neothrombolytika speziell mit Gewebeplasminogenaktivator, Prourokinase und deren KombinationenHamostaseologie, 1988
- Human tissue-type plasminogen activator. Production in continuous serum-free cell culture and rapid purificationBiochemical Journal, 1985
- Studies on the kinetics of plasminogen activation by tissue plasminogen activatorBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Purification of rat fibrinogen and its constituent chainsBiochemical Journal, 1978
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976