Ion-exchange chromatography separation of the detergent and the solvent from immunoglobulins after solvent-detergent treatment

Citation
B. Gebauer et al., Ion-exchange chromatography separation of the detergent and the solvent from immunoglobulins after solvent-detergent treatment, J CHROMAT A, 852(1), 1999, pp. 83-86
Citations number
14
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis","Spectroscopy /Instrumentation/Analytical Sciences
Journal title
JOURNAL OF CHROMATOGRAPHY A
ISSN journal
0021-9673 → ACNP
Volume
852
Issue
1
Year of publication
1999
Pages
83 - 86
Database
ISI
SICI code
0021-9673(19990806)852:1<83:ICSOTD>2.0.ZU;2-D
Abstract
For inactivation of lipid-enveloped viruses during the immunoglobulin produ ction, the solvent-detergent (S/D) method was applied. Tri-n-butyl phosphat e (solvent) and Triton X-100 (detergent) were removed from S/D treated immu noglobulins by ion-exchange chromatography on Q-Sepharose Fast Flow (FF). D uring the chromatographic procedure immunoglobulins remained bound on a Q-S epharose EF, whereas solvent and detergent were eluted by washing with star ting buffer. Elution of immunoglobulins was achieved by increasing the ioni c strength of the starting buffer. The final immunoglobulin preparation con tained less than 10 mu g/ml of Triton X-100 and less than 2 mu g/ml tri-n-b utyl phosphate. It was confirmed that the S/D procedure did not cause a sig nificant change in polymers and specific antibodies content. Immunoglobulin classes were also not affected by the same procedure. (C) 1999 Elsevier Sc ience B.V. All rights reserved.