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-Reference-Cited by-同舟云学术

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

Published:1993-11 Issue:6 Volume:7 Page:365-372
ISSN:0268-9499
Container-title:Fibrinolysis
language:en
Short-container-title:Fibrinolysis

Author:

Kohnert U.,Horsch B.,Fischer S.

Publisher

Elsevier BV

Subject

Hematology

Reference18 articles.

1. Gewebs-Plasminogenaktivator-Derivat;Stern,1989

2. Biochemical properties of the kringle 2 and protease domains are maintained in the refolded t-PA deletion variant BM 06.022;Kohnert;Protein Eng,1992

3. On the interaction of the finger and the kringle 2 domain of tissuetype plasminogen activator with fibrin;van Zonneveld;J Biol Chem,1986

4. Thrombolysis with an Escherichia coli-produced recombinant plasminogen activator (BM 06.022) in the rabbit model of jugular vein thrombosis;Martin;Thromb Haemost,1991

5. Kinetics of the tissue-type plasminogen activator mediated activation of plasminogen. The influence of CNBr fibrin(ogen) fragment FCB-2 and different forms of plasminogen;Nieuwenhuizen,1985

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