high quality human immunoglobulin g purified from cohn fractions by liquid chromatography

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ID: 192488
2000
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Abstract
In order to obtain intravenous immunoglobulin G (iv IgG) of high quality from F-I+II+III or F-II+III pastes prepared by the Cohn method, we developed a chromatography process using ion exchange gels, Q-Sepharose FF and CM-Sepharose FF, and Sephacryl S-300 gel filtration. Viral inactivation was performed by incubating the preparation with pepsin at pH 4.0 at 35oC for 18 h. The characteristics of 28 batches produced by us were: yield 4.3 ± 0.2 g/l plasma, i.e., a recovery of 39.1 ± 1.8%; IgG subclasses distribution: IgG1 = 58.4%, IgG2 = 34.8%, IgG3 = 4.5% and IgG4 = 2.3%; IgG size distribution was 98.4% monomers, 1.2% dimers and 0.4% polymers and protein aggregates; anticomplement activity was less than 0.5 CH50/mg IgG, and prekallikrein activator activity (PKA) was less than 5 IU/ml. These characteristics satisfied the requirements of the European Pharmacopoea edition, and the regulations of the Brazilian Health Ministry (M.S. Portaria No. 2, 30/10/1998).
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tanaka2000brazilianhigh Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;K. Tanaka;E. Sawatani;G.A. Dias;E.M. Shigueoka;T.C.X.B. Campos;H.C. Nakao;F. Arashiro
Journal Free radical biology & medicine
Year 2000
DOI
10.1590/S0100-879X2000000100004
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