2002
DOI: 10.1046/j.1423-0410.2002.00241.x
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Purification of human immunoglobulin G: a new approach to plasma fractionation

Abstract: The technology has been shown to be linearly scalable and has the capacity to contribute to increased production of important plasma fraction therapeutics.

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Cited by 45 publications
(29 citation statements)
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“…Currently the large-scale purification of polyclonal antibodies is, for the most part, carried out by the plasma fractionation industry, with production being geared towards generation of a wide range of plasma proteins (including albumin, Factor VIII, Factor IX, Protein C and von Willebrand Factor) rather than single antibody products [1][2][3]. Since the first reports on the use of immobilised Protein A for the affinity purification of antibodies over 30 years ago [4,5].…”
Section: Introductionmentioning
confidence: 99%
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“…Currently the large-scale purification of polyclonal antibodies is, for the most part, carried out by the plasma fractionation industry, with production being geared towards generation of a wide range of plasma proteins (including albumin, Factor VIII, Factor IX, Protein C and von Willebrand Factor) rather than single antibody products [1][2][3]. Since the first reports on the use of immobilised Protein A for the affinity purification of antibodies over 30 years ago [4,5].…”
Section: Introductionmentioning
confidence: 99%
“…Since the first reports on the use of immobilised Protein A for the affinity purification of antibodies over 30 years ago [4,5]. Protein A affinity chromatography has become the industrial standard for the purification of clinical grade monoclonal antibodies [3,[6][7][8], but is rarely applied in the plasma fractionation industry [1,2], largely for reasons of cost and reservations concerning Protein A's chemical stability, adsorbent shelf-life and cleaning [9]. For the production of diagnostic antibody products such concerns are less serious; thus Protein A chromatography currently represents one of most potent separation tools available to the diagnostic industry.…”
Section: Introductionmentioning
confidence: 99%
“…Immediately after, the cell suspension was incubated under lateral agitation (CAT model M5, CAT Ingenieurburo, Staufen, DE) at a rate of 36 rpm for 1 h at 37°C. This second mixing was performed at room temperature (RT°; 25°C) for the homopolymers, whereas for the copolymers, three distinct temperatures (25,30, and 37°C) have been investigated. After that, 1 mL of PBS was added to the treated RBCs to wash and centrifuge them (Mini Spin Plus Microcentrifuge, Eppendorf) for 10 min at 600 rpm.…”
Section: Methodsmentioning
confidence: 99%
“…The electrodes prepared with 48 pmol of nanoparticles provided the highest immobilized yield 88.2-88.6% (3.5 × 10 13 molecules, calculated using a molecular weight of 150 kDa for an IgG [28,29]). This agreed well with the larger surface area as indicated by the higher anodic peak current.…”
Section: Immobilization Yieldmentioning
confidence: 99%