Dissociation of aggregated IgG and denaturation of monomeric IgG by acid treatment.

Uemura, Yahiro

doi:10.1620/tjem.141.337

Cited by 9 publications

(7 citation statements)

References 24 publications

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“…No binding of either native or pH 3.5/4 acid‐shocked CH3 to IgG was observed, whereas an acid shock of pH 3 or lower resulted in increased probe binding to IgG. These results confirm the pH‐dependent effects described by Uemura 8. Under the influence of low pH treatment (below pH 3), the CH3 domains of the probe dissociate.…”

Section: Discussionsupporting

confidence: 84%

“…During the IVIg manufacturing process, pH 4 or higher is used. This pH causes the dissociation of IgG aggregates present in IVIg 8. Consequently, there are three possibilities regarding the formation of these alternatively folded monomeric IgG molecules.…”

Section: Discussionmentioning

confidence: 99%

“…Ahrer et al7 reported that the amount of dimers and aggregates in IVIg depends on the variations of manufacturing process conditions such as pH, flow rate, and mixing speed. Another study showed that at a pH between 3.8 and 4, most aggregates present in IVIg dissociate, whereas a pH treatment below 3.8 results in IgG aggregation due to acid denaturation of IgG 8. By using a monoclonal mouse anti‐rat antibody, Vermeer and Norde9 demonstrated that this pH‐induced denaturation is mainly seen in the Fc region.…”

Section: Introductionmentioning

confidence: 99%

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Use of a Human Recombinant Immunoglobulin G1 CH3 Domain as a Probe for Detecting Alternatively Folded Human IgG in Intravenous Ig Products

Guhr

Derksen

Aalberse

et al. 2012

Journal of Pharmaceutical Sciences

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Section: Discussionsupporting

confidence: 84%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Use of a Human Recombinant Immunoglobulin G1 CH3 Domain as a Probe for Detecting Alternatively Folded Human IgG in Intravenous Ig Products

Guhr

Derksen

Aalberse

et al. 2012

Journal of Pharmaceutical Sciences

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“…The treatment at low pH was originally developed to disaggregate reversible IgG polymers. At low pH IgG molecules are highly positively charged and thus aggregates are separated by electrostatic repulsion [104]. This does not work for already denatured aggregates.…”

Section: Treatment At Low Phmentioning

confidence: 99%

Purification of intravenous immunoglobulin G from human plasma – aspects of yield and virus safety

Buchacher

Iberer

2006

Biotechnology Journal

110

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Plasma-derived intravenous immunoglobulin (IVIG) preparations have been successfully applied for the prophylactic prevention of infectious diseases in immunodeficient patients. In addition to its replacement therapy of primary and secondary antibody deficiencies, IVIG has found increased use in autoimmune and inflammatory diseases. IVIG has become the major plasma product on the global blood product market. The world wide consumption nearly tripled between 1992 and 2003, from 19.4 to 52.6 tons. Classical manufacturing processes of IVIG, but also new strategies for purification are discussed with respect to practicability and yield. Ethanol fractionation is still the basis for most IVIG processes, although isolation and purification of immunoglobulin G (IgG) by chromatography has gained ground. The efficiency of virus inactivation methods and virus removal techniques in terms of logarithmic reduction factors are analyzed, but also the IgG losses are taken into consideration. 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.

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“…IgG monomer was obtained from Fr-II by gel filtration on a Sephadex G-200 column [8], Gammavenin (Hoechst Japan Co. Ltd., Tokyo) and Venilon (Teijin Co. Ltd., Tokyo) were used as a F(ab')2 fragment and a sulfonated IVIG(IVIG-S), respectively.…”

Section: Human Igg Fractionsmentioning

confidence: 99%

Inactivation and Elimination of Viruses during the Fractionation of an Intravenous Immunoglobulin Preparation: Liquid Heat Treatment and Polyethylene Glycol Fractionation

Uemura¹,

Uriyu²,

Hirao³

et al. 1989

Vox Sanguinis

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A method for the heat treatment of human IgG solution at 60 °C for 10 h was established. Human immunodeficiency, mumps, vaccinia and 4 other viruses were added to the IgG solution in 33% sorbitol and heated at 60 °C. Those viruses were inactivated within 1 h. Heat-treated intravenous IgG (IVIG-H) was prepared by heat treatment and polyethylene glycol (PEG) fractionation. Conventional nonheated intravenous IgG (IVIG-C) was prepared from the same source paste by the fractionation method. No physicochemical or biological difference was observed between the heated and control IVIG preparations.

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Dissociation of aggregated IgG and denaturation of monomeric IgG by acid treatment.

Cited by 9 publications

References 24 publications

Use of a Human Recombinant Immunoglobulin G1 CH3 Domain as a Probe for Detecting Alternatively Folded Human IgG in Intravenous Ig Products

Use of a Human Recombinant Immunoglobulin G1 CH3 Domain as a Probe for Detecting Alternatively Folded Human IgG in Intravenous Ig Products

Purification of intravenous immunoglobulin G from human plasma – aspects of yield and virus safety

Inactivation and Elimination of Viruses during the Fractionation of an Intravenous Immunoglobulin Preparation: Liquid Heat Treatment and Polyethylene Glycol Fractionation

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