Quality assessment and optimization of purified protein samples: why and how?

Microbial Cell Factories

Review

Patrick England¹  Pascal Lenormand¹  Bruno Baron¹  Bertrand Raynal¹  Sylviane Hoos¹ 

[1] Institut Pasteur, Biophysics of Macromolecules and their Interactions, 25 rue du Docteur Roux, 75724, Paris Cedex 15, France;CNRS-UMR3528, Institut Pasteur, Departement of Structural Biology and Chemistry, Paris, France;

关键词: Recombinant protein;    Therapeutic;    Diagnosis;    Structural biology;    Electrophoresis;    Mass spectrometry;    UV/visible spectroscopy;    Light scattering;    Size-exclusion chromatography;    Surface plasmon resonance;    Formulation;    Comparability;   

DOI  :  10.1186/s12934-014-0180-6

 received in 2014-09-25, accepted in 2014-12-10,  发布年份 2014

来源: Springer

【 摘 要 】

Purified protein quality control is the final and critical check-point of any protein production process. Unfortunately, it is too often overlooked and performed hastily, resulting in irreproducible and misleading observations in downstream applications. In this review, we aim at proposing a simple-to-follow workflow based on an ensemble of widely available physico-chemical technologies, to assess sequentially the essential properties of any protein sample: purity and integrity, homogeneity and activity. Approaches are then suggested to optimize the homogeneity, time-stability and storage conditions of purified protein preparations, as well as methods to rapidly evaluate their reproducibility and lot-to-lot consistency.

【 授权许可】

CC BY   
© Raynal et al.; licensee BioMed Central. 2014