Autor: Ciach, Tomasz - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: The factor VIII protein and its function
Autorzy:: Mazurkiewicz-Pisarek, Anna
Płucienniczak, Grażyna
Ciach, Tomasz
Płucienniczak, Andrzej
Powiązania:: https://bibliotekanauki.pl/articles/1038835.pdf
Data publikacji:: 2016
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: Factor VIII (FVIII)
molecular structure
function
hemophilia A
bleeding disorders
Opis:: Factor VIII (FVIII), an essential blood coagulation protein, is a key component of the fluid phase blood coagulation system. Human factor VIII is a single chain of about 300 kDa consisting of domains described as A1-A2-B-A3-C1-C2. The protein undergoes processing prior to secretion into blood resulting in a heavy chain of 200 kDa (A1-A2-B) and a light chain of 80 kDa (A3-C1-C2) linked by metal ions. The role of factor VIII is to increase the catalytic efficiency of factor IXa in the activation of factor X. Variants of these factors lead frequently also to severe bleeding disorders.
Źródło:: Acta Biochimica Polonica; 2016, 63, 1; 11-16
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: Expression of the gene encoding blood coagulation factor VIII without domain B in E. coli bacterial expression system
Autorzy:: Mazurkiewicz-Pisarek, Anna
Mazurkiewicz, Alina
Mikiewicz, Diana
Baran, Piotr
Ciach, Tomasz
Powiązania:: https://bibliotekanauki.pl/articles/16706242.pdf
Data publikacji:: 2023
Wydawca:: Polska Akademia Nauk. Czasopisma i Monografie PAN
Tematy:: factor VIII
hemophilia type A
recombinant coagulation factor VIII
prokaryotic expression system
E. coli
recombinant protein production system
Opis:: In this article, we have demonstrated the feasibility of generating an active form of recombinant blood coagulation factor VIII using an E. coli bacterial expression system as a potential treatment for hemophilia type A. Factor VIII (FVIII), an essential blood coagulation protein, is a key component of the fluid phase blood coagulation system. So far, all available recombinant FVIII formulations have been produced using eukaryotic expression systems. Mammalian cells can produce catalytically active proteins with all the necessary posttranslational modifications. However, cultivating such cells is time-consuming and highly expensive, and the amount of the obtained product is usually low. In contrast to eukaryotic cells, bacterial culture is inexpensive and allows the acquisition of large quantities of recombinant proteins in a short time. With this study, we aimed to obtain recombinant blood coagulation factor VIII using the E. coli bacterial expression system, a method not previously explored for this purpose. Our research encompasses the synthesis of blood coagulation factor VIII and its expression in a prokaryotic system. To achieve this, we constructed a prokaryotic expression vector containing a synthetic factor VIII gene, which was then used for the transformation of an E. coli bacterial strain. The protein expression was confirmed by mass spectrometry, and we assessed the stability of the gene construct while determining the optimal growth conditions. The production of blood coagulation factor VIII by the E. coli bacterial strain was carried out on a quarter-technical scale. We established the conditions for isolation, denaturation, and renaturation of the protein, and subsequently confirmed the activity of FVIII.
Źródło:: BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2023, 104, 3; 247-262
0860-7796
Pojawia się w:: BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:: Biblioteka Nauki

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