Production and Purification of Recombinant Proteins

Kadir, F.; Ives, P. M.; Luitjens, Alfred; Corven, Emile van

doi:10.1007/978-1-4614-6486-0_3

Cited by 4 publications

(2 citation statements)

References 22 publications

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“…Similar to other biologics, mAbs are produced batch‐wise in living cells. As such, they are defined by the production process rather than their chemical structure, and batch‐to‐batch variability in the resulting product is well recognized and needs to be tightly controlled through carefully established and controlled conditions during the cell culturing, product processing, and purification steps …”

Section: Structure and Originmentioning

confidence: 99%

Pharmacokinetics of Monoclonal Antibodies

Ryman

Meibohm

2017

CPT Pharmacom & Syst Pharma

584

547

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Monoclonal antibodies (mAbs) have developed in the last two decades into the backbone of pharmacotherapeutic interventions in a variety of indications, with currently more than 40 mAbs approved by the US Food and Drug Administration, and several dozens more in clinical development. This tutorial will review major drug disposition processes relevant for mAbs, and will highlight product‐specific and patient‐specific factors that modulate their pharmacokinetic (PK) behavior and need to be considered for successful clinical therapy.

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Section: Structure and Originmentioning

confidence: 99%

Pharmacokinetics of Monoclonal Antibodies

Ryman

Meibohm

2017

CPT Pharmacom & Syst Pharma

584

547

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“…It indicates that even if the host cell has a capability of a specific post-translation modification such as glycosylation, still there is a possibility of a difference in the pattern of glycosylation compared to the native protein. To retain the stability, immunogenicity, biological activity, and pharmacokinetic behavior of a therapeutic protein, its N-linked glycosylation pattern should be correct [14]. Some general considerations and requirements for the proficient production of recombinant protein are described in Figure 2.…”

Section: Ls-731 Figures To Be Replacedmentioning

confidence: 99%

Comparison of Host Expression Systems used for Efficient Recombinant Proteins Production

Mukhtar

Sahreen

Sharif

et al. 2023

PPASB

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The marvels of DNA recombination technology have revolutionized the field of biotechnology. Several hormones, antibody subunits, vaccines, enzymes, and interferons are being produced at the industrial level, in suitable expression systems, under optimized conditions. For recombinant protein production, a range of expression systems are available such as bacteria, yeast, fungi, plant cells, insects and animal cells, etc. Each recombinant protein has different nature due to which it requires different challenges regarding the expression system and production conditions. Every expression system has its advantages and limitations on the basis of which it can be considered or rejected for a particular protein production. Therefore, it is very significant to investigate the potential and limitations of several expression systems to choose the suitable one for particular protein production at an industrial scale. The optimization criteria of an expression system is evaluated on several factors such as productivity, efficiency, physiological characteristics, total cost, safety, convenience, and down-streaming conditions. Escherichia coli and Saccharomyces cerevisiae remained the organisms of choice to produce recombinant proteins for a long time, but now several other microorganisms are also being targeted to evaluate their efficiency toward recombinant protein production. Prokaryotic expression systems can be used to produce eukaryotic proteins as well however, the use of a eukaryotic expression system is preferable because it retains the structural, functional, and regulatory properties of therapeutic proteins. This review illustrates a brief view of a variety of expression systems, their efficiency, and limitations in recombinant protein production.

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Production and Application of Novel Bio-active Compounds by Endophytic Microbes

Filho

2019

Natural Bio-Active Compounds

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Production and Purification of Recombinant Proteins

Cited by 4 publications

References 22 publications

Pharmacokinetics of Monoclonal Antibodies

Pharmacokinetics of Monoclonal Antibodies

Comparison of Host Expression Systems used for Efficient Recombinant Proteins Production

Production and Application of Novel Bio-active Compounds by Endophytic Microbes

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