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Details

Autor(en) / Beteiligte
Titel
A simple method for large-scale purification of plasma-derived apo-transferrin
Ist Teil von
  • Biotechnology and applied biochemistry, 2010-11, Vol.57 (3), p.87-95
Ort / Verlag
Oxford, UK: Blackwell Publishing Ltd
Erscheinungsjahr
2010
Quelle
Wiley-Blackwell Journals
Beschreibungen/Notizen
  • We investigated and optimized a purification process, suitable for industrial scale, to obtain pharmaceutical grade apo‐Tf (apo‐transferrin), preserving its physiological properties and functions. Apo‐Tf was obtained from fraction IV subfraction 1 and IV subfraction 4 (fraction IV‐1,4), a waste product of the Cohn fractionation process, performing a single chromatographic run and two viral inactivation/removal steps. The structural integrity and the biological activity of the final product were extensively tested. The yield of apo‐Tf produced was 80% on laboratory scale and 90% in scale‐up lots, and the purity was higher than 95%. The purified protein preserves iron‐ and receptor‐binding activities and shows a normal glycosylation pattern. The single chromatographic step process presented here provides an efficient means to prepare commercial quantities of the protein. The final product is sterile and two viral inactivation/removal steps were introduced into the process.

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