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Siti Najila Mohd Janib; Wan Hamirul Bahrin Wan Kamal; Shaharuddin Mohd
Proceedings of the MINT R and D Seminar 2004: Innovation through excellence in R and D, Seminar A2004
Proceedings of the MINT R and D Seminar 2004: Innovation through excellence in R and D, Seminar A2004
AbstractAbstract
[en] Chromatography is a powerful technique used in the separation as well as purification of proteins for use as biopharmaceuticals or medicines. Scientists use many different chromatographic techniques in biotechnology as they bring a molecule from its initial identification stage to the stage of it becoming a marketed product. The most commonly used of these techniques is liquid chromatography (1,C). This technique can be used to separate the target molecule from undesired contaminants, as well as to analyse the final product for the requisite purity as established by governmental regulatory groups such as the FDA. Some examples of LC techniques include: ion exchange (IEC), hydrophobic interaction (HIC), gel filtration (GF), affinity (AC) and reverse phase (RPC) chromatography. These techniques are very versatile and can be used at any stage of the purification process i.e. capture, intermediate purification phase and polishing. The choice of a particular technique is dependent upon the nature of the target protein as well as its intended final use. This paper describes the preliminary work done on the chromatographic purification of factor VIII (FVIII), factor IX (FIX), albumin and IgG from plasma. Results, in particular, in the isolation of albumin and IgG using IEC, have been promising. Preparation and production of cryoprecipitate to yield FVIII and FIX have also been successful. (Author)
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Malaysian Inst. for Nuclear Technology Research MINT, Bangi (Malaysia); 291 p; 2004; p. 92-98; Seminar MINT R and D 2004; Bangi (Malaysia); 12-15 Jul 2004; Available at Malaysian Inst. for Nuclear Technology Research MINT, Bangi, Malaysia; Ainon@mint.gov.my
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Miscellaneous
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Conference
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