Pregled bibliografske jedinice broj: 951915
Ion-exchange chromatography using CIM QA as a final polishing step in horse F(ab’)2-based immunotherapeutics preparation
Ion-exchange chromatography using CIM QA as a final polishing step in horse F(ab’)2-based immunotherapeutics preparation // Monolith Summer School and Symposium
Portorož, Slovenija, 2018. str. 45-45 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 951915 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Ion-exchange chromatography using CIM QA as a final polishing step in horse F(ab’)2-based immunotherapeutics preparation
Autori
Kurtović, Tihana ; Brgles, Marija ; Halassy, Beata
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Monolith Summer School and Symposium
/ - , 2018, 45-45
Skup
Monolith Summer School and Symposium
Mjesto i datum
Portorož, Slovenija, 15.06.2018. - 20.06.2018
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
antivenom ; immunoglobulin purification ; CIM QA chromatography
Sažetak
Horse F(ab')2-based biomedicines are the only effective and specific therapy against snakebite. In general, F(ab')2 are produced by pepsin hydrolysis of immunoglobulin G molecules since Fc removal reduces their side-effects-inducing potential, thus generating drug of improved safety more suitable for use in human. The final product should be free of residual contaminants from fractionation process, thus, elimination of pepsin - the main stability-compromising agent, should be guaranteed. This study aimed to investigate the possibility of employing ion-exchange chromatography using CIM QA disk as a method of choice for the final polishing - removal of any processing by-product traces, primarily pepsin. Namely, development of our F(ab’)2 purification processing strategy has been guided by the imperative of constantly keeping active compound (IgG or F(ab’)2) in solution, since possible degradation/aggregation due to precipitation or binding to chromatographic support might lead to reduced efficacy and/or stability of the final product. We have successfully developed chromatographic conditions enabling complete binding of pepsin to CIM QA disk, while leaving F(ab’)2 fragments in the flow through fraction. The yield of the final polishing by the novel method is near 100%. Described chromatographic procedure was also shown to be applicable for further purification of commercial pepsin preparation that is often contaminated with non-enzymatically active material.
Izvorni jezik
Engleski
Znanstvena područja
Biotehnologija u biomedicini (prirodno područje, biomedicina i zdravstvo, biotehničko područje)
POVEZANOST RADA
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