Subtitle:

Construction of synthetic gene coding for K2L-tPA - deletion variant of tissue plasminogen activator. Expression in E. coli and renaturation of recombinant protein

Publisher:

Committee on Biotechnology PAS ; Institute of Bioorganic Chemistry PAS

Abstract:

The human fibrinolytic system comprises an inactive proenzyme -plasminogen which can be converted to the active form - plasmin which, in turn,degrades fibrin clots into soluble fibrin degradation products. Tissue plasminogenactivator (t-PA) has been identified as a main physiological factor responsible forplasminogen - plasmin conversion. The high fibrin specificity of t-PA, which allows efficient activation on the surface of fibrin clots, has stimulated great interestin its preparation to be used for thrombolytic therapy. Several approaches havebeen followed to further improve the thrombolytic properties of recombinant t-PAby protein engineering to enhance its plasminogen - activating potency as well asfibrin specificity, and to reduce its plasma clearance. One of the approaches involves the conjugation of its deletion variant, so-called K2L-tPA, to various biomolecules. K2L-tPA is a 351-aminoacid C-terminal fragment of human t-PA. The protein is composed of two major domains; Kringle-2 (K2), responsible for fibrin binding, and so-called Light Chain domain (L), containing active centre ofthe enzyme. Inthis paper, we describe our efforts on expression of synthetic gene coding forK2L-tPA, and on renaturation and purification of recombinant protein

Relation:

Biotechnologia, vol.63, 4 (2003)-.

Volume:

63

Issue:

4

Start page:

124

End page:

141

Detailed Resource Type:

Article

Format:

application/pdf

Resource Identifier:

0860-7796 ; oai:rcin.org.pl:129765 ; IChB B-59

Source:

Library of Institute of Bioorganic Chemistry PAS

Language:

pol

Language of abstract:

eng

Temporal coverage:

1988-2010

Rights:

Creative Commons Attribution BY-SA 4.0 license

Terms of use:

Copyright-protected material. [CC BY-SA 4.0] May be used within the scope specified in Creative Commons Attribution BY-SA 4.0 license, full text available at:

Digitizing institution:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Original in:

Institute of Bioorganic Chemistry of the Polish Academy of Science

Projects co-financed by:

Operational Program Digital Poland, 2014-2020, Measure 2.3: Digital accessibility and usefulness of public sector information; funds from the European Regional Development Fund and national co-financing from the state budget.

Access:

Open