@misc{Sierant_Małgorzata_Construction_2003,
 author={Sierant, Małgorzata and Okruszek, Andrzej},
 volume={63},
 number={4},
 copyright={Creative Commons Attribution BY-SA 4.0 license},
 journal={Biotechnologia, vol.63, 4 (2003)-.},
 howpublished={online},
 year={2003},
 publisher={Committee on Biotechnology PAS},
 publisher={Institute of Bioorganic Chemistry PAS},
 language={pol},
 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},
 type={Text},
 title={Construction of synthetic gene coding for K2L-tPA - deletion variant of tissue plasminogen activator. Expression in E. coli and renaturation of recombinant protein},
 URL={http://rcin.org.pl/Content/129765/PDF/POZN271_162479_biotechnologia-2003-no4-sierant.pdf},
 keywords={biotechnology},
}