Viral Infectivity of Albumin and Plasma Protein Fraction

Erstad, Brian L.

doi:10.1002/j.1875-9114.1996.tb03024.x

Cited by 29 publications

(1 citation statement)

References 32 publications

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“…Other applications for HSA include the nanocarrier of drugs [ 21 ], the carrier of oxygen [ 22 ], and extending the plasma half-life of target proteins [ 23 ]. The production of HSA is mainly based on collected human plasma, with all the associated limitations in the supply and potential blood-derived infectious pathogen contamination (such as hepatitis and HIV) [ 24 , 25 ]. Hence, to avoid dependence on pooled human blood products, in the last few decades, the production of HSA was examined by recombinant DNA technology using different host systems like Escherichia coli , Pichia pastoristext , Saccharomyces cerevisiae , Kluyveromyces lactis , transgenic animals, and plants [ 26 , 27 , 28 , 29 , 30 , 31 ].…”

Section: Introductionmentioning

confidence: 99%

Simultaneous Purification of Human Interferon Alpha-2b and Serum Albumin Using Bioprivileged Fluorinated Ionic Liquid-Based Aqueous Biphasic Systems

Carvalho,

Pereiro,

Araújo

2024

IJMS

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Interferon alpha-2b (IFN-α2b) is an essential cytokine widely used in the treatment of chronic hepatitis C and hairy cell leukemia, and serum albumin is the most abundant plasma protein with numerous physiological functions. Effective single-step aqueous biphasic system (ABS) extraction for the simultaneous purification of IFN-α2b and BSA (serum albumin protein) was developed in this work. Effects of the ionic liquid (IL)-based ABS functionalization, fluorinated ILs (FILs; [C2C1Im][C4F9SO3] and [N1112(OH)][C4F9SO3]) vs. mere fluoro-containing IL ([C4C1Im][CF3SO3]), in combination with sucrose or [N1112(OH)][H2PO4] (well-known globular protein stabilizers), or high-charge-density salt K3PO4 were investigated. The effects of phase pH, phase water content (%wt), phase composition (%wt), and phase volume ratio were investigated. The phase pH was found to have a significant effect on IFN-α2b and BSA partition. Experimental results show that simultaneous single-step purification was achieved with a high yield (extraction efficiency up to 100%) for both proteins and a purification factor of IFN-α2b high in the enriched IFN-α2b phase (up to 23.22) and low in the BSA-enriched phase (down to 0.00). SDS-PAGE analysis confirmed the purity of both recovered proteins. The stability and structure of IFN-α2b and BSA were preserved or even improved (FIL-rich phase) during the purification step, as evaluated by CD spectroscopy and DSC. Binding studies of IFN-α2b and BSA with the ABS phase-forming components were assessed by MST, showing the strong interaction between FILs aggregates and both proteins. In view of their biocompatibility, customizable properties, and selectivity, FIL-based ABSs are suggested as an improved purification step that could facilitate the development of biologics.

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Section: Introductionmentioning

confidence: 99%

Simultaneous Purification of Human Interferon Alpha-2b and Serum Albumin Using Bioprivileged Fluorinated Ionic Liquid-Based Aqueous Biphasic Systems

Carvalho,

Pereiro,

Araújo

2024

IJMS

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Plants as Bioreactors

Madhu¹,

Sharma²,

Kaur³

et al. 2023

Plants as Bioreactors for Industrial Molecules

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Emerging trends in plasma‐free manufacturing of recombinant protein therapeutics expressed in mammalian cells

Grillberger

Kreil

Nasr³

et al. 2009

Biotechnology Journal

134

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Mammalian cells are the expression system of choice for therapeutic proteins, especially those requiring complex post-translational modifications. Traditionally, these cells are grown in medium supplemented with serum and other animal-or human-derived components to support viability and productivity. Such proteins are also typically added as excipients and stabilizers in the final drug formulation. However, the transmission of hepatitis B in the 1970s and of hepatitis C and HIV in the 1980s through plasma-derived factor VIII concentrates had catastrophic consequences for hemophilia patients. Thus, due to regulatory concerns about the inherent potential for transmission of infectious agents as well as the heterogeneity and lack of reliability of the serum supply, a trend has emerged to eliminate the use of plasma-derived additives in the production and formulation of recombinant protein therapeutics. This practice began with products used in the treatment of hemophilia and is progressively expanding throughout the entire industry. The plasma-free method of producing recombinant therapeutics is accomplished by the use of both cell culture media and final product formulations that do not contain animal-or human-derived additives. A number of recombinant therapeutic proteins for the treatment of several different diseases have been produced by plasma-free processes, with the objective of improving safety by eliminating blood-borne pathogens or by reducing immunogenicity. This review describes the factors that drove the development of plasma-free protein therapeutics and provides examples of advances in manufacturing that have made possible the removal of human and animal-derived products from all steps of recombinant protein production.

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Viral Infectivity of Albumin and Plasma Protein Fraction

Cited by 29 publications

References 32 publications

Simultaneous Purification of Human Interferon Alpha-2b and Serum Albumin Using Bioprivileged Fluorinated Ionic Liquid-Based Aqueous Biphasic Systems

Simultaneous Purification of Human Interferon Alpha-2b and Serum Albumin Using Bioprivileged Fluorinated Ionic Liquid-Based Aqueous Biphasic Systems

Plants as Bioreactors

Emerging trends in plasma‐free manufacturing of recombinant protein therapeutics expressed in mammalian cells

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