Research Topics
| Andrea BuchacherSummaryAffiliation: Pre-Clinical Research and Development Country: Austria Publications
| Collaborators
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Detail Information
Publications
Continuous removal of protein aggregates by annular chromatographyA Buchacher
Octapharma Pharmazeutische ProduktionsGes m b H, Oberlaaerstrasse 235, A 1100 Vienna, Austria
Biotechnol Prog 17:140-9. 2001..We have demonstrated that size exclusion can be performed on an industrial scale when it is run continuously with the aid of a pressurized annular chromatograph...
Purification of intravenous immunoglobulin G from human plasma--aspects of yield and virus safetyAndrea Buchacher
Octapharma Pharmazeutika Produktions GmbH, Oberlaaerstrasse 235, 1100 Vienna, Austria
Biotechnol J 1:148-63. 2006..Some of these methods also have the ability to separate prions. High pathogen safety and high yields have become the dominant goals of the plasma fractionation industry...
Anticomplementary activity of IVIG concentrates--important assay parameters and impact of IgG polymersA Buchacher
Octapharma Pharmazeutika ProduktionsGmbH, Vienna, Austria
Vox Sang 98:e209-18. 2010..The goal of this study was to scrutinize critical parameters of the ACA assay and the influence of different polymer variants of IgG on the complement consumption...
Preparation of vitamin K-dependent proteins, such as clotting factors II, VII, IX and X and clotting inhibitor protein CDjuro Josic
Octapharma Pharmazeutika Produktions Ges m b H, Oberlaaerstrasse 235, A 1100, Vienna, Austria
J Chromatogr B Analyt Technol Biomed Life Sci 790:183-97. 2003..The methods for their purification are described. The problem of difference in posttranslational modifications between plasma derived and recombinant protein is discussed with regard to therapeutic proteins...
Separation of active and inactive forms of human antithrombin by heparin affinity chromatographyAndrea Heger
Research and Development, Octapharma Pharmazeutika Produktionsges m b H, Oberlaaer Strasse 235, A 1100 Vienna, Austria
Thromb Res 106:157-64. 2002..In four commercially available antithrombin preparations, all produced by pasteurization, the amount of inactive protein varied between 0.5% and 9.5%...
Characterization of antithrombin III from human plasma by two-dimensional gel electrophoresis and capillary electrophoretic methodsLeopold Kremser
Institute of Analytical Chemistry, University of Vienna, Vienna, Austria
Electrophoresis 24:4282-90. 2003..6% of ATIII-beta. The pI values of ATIII determined by CIEF with internal calibration were in fair agreement with the pI values of the main isoforms achieved with 2-DE...
Isolation of esterified fatty acids bound to serum albumin purified from human plasma and characterised by MALDI mass spectrometryOmar Belgacem
Octapharma Pharmazeutika, Oberlaaer Str 235, A 1100 Vienna, Austria
Biologicals 35:43-9. 2007..Besides the native ligands from plasma a triacylglycerol was detected that has been added during the albumin preparation steps...
Molecular mass determination of plasma-derived glycoproteins by ultraviolet matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with internal calibrationOmar Belgacem
Institute for Analytical Chemistry, University of Vienna, , A-1090 Vienna, Austria
J Mass Spectrom 37:1118-30. 2002..41 kDa, corresponding to V65 and V10 subunits of VN. PNGase F digest of the V75 and V65 units and MS analysis, exhibiting a molecular mass reduction of 6.37 kDa in both cases, verified the presence of a considerable amount of N-glycans...
Exact molecular mass determination of various forms of native and de-N-glycosylated human plasma-derived antithrombin by means of electrospray ionization ion trap mass spectrometryMartina Kleinova
Institute of Chemical Technologies and Analysis, Vienna University of Technology, Getreidemarkt 9/164, A-1060 Vienna, Austria
J Mass Spectrom 39:1429-36. 2004..The determined molecular masses after reduction/alkylation and de-N-glycosylation of the alpha-and beta-forms are almost equal, indicating that no major differences exist between the three preparations on the amino acid level...
