caa a22 4500 463186478 CHVBK 20180406164854.0 cr unu---uuuuu 170326e20071101xx s 000 0 eng 10.1007/s00726-007-0506-3 doi (NATIONALLICENCE)springer-10.1007/s00726-007-0506-3 Biotechnology applications of amino acids in protein purification and formulations [Elektronische Daten] [T. Arakawa, K. Tsumoto, Y. Kita, B. Chang, D. Ejima] Summary.: Amino acids are widely used in biotechnology applications. Since amino acids are natural compounds, they can be safely used in pharmaceutical applications, e.g., as a solvent additive for protein purification and as an excipient for protein formulations. At high concentrations, certain amino acids are found to raise intra-cellular osmotic pressure and adjust to the high salt concentrations of the surrounding medium. They are called "compatible solutes”, since they do not affect macromolecular function. Not only are they needed to increase the osmotic pressure, they are known to increase the stability of the proteins. Sucrose, glycerol and certain amino acids were used to enhance the stability of unstable proteins after isolation from natural environments. The mechanism of the action of these protein-stabilizing amino acids is relatively well understood. On the contrary, arginine was accidentally discovered as a useful reagent for assisting in the refolding of recombinant proteins. This effect of arginine was ascribed to its ability to suppress aggregation of the proteins during refolding, thereby increasing refolding efficiency. By the same mechanism, arginine now finds much wider applications than previously anticipated in the research and development of proteins, in particular in pharmaceutical applications. For example, arginine solubilizes proteins from loose inclusion bodies, resulting in efficient production of active proteins. Arginine suppresses protein-protein interactions in solution and also non-specific adsorption to gel permeation chromatography columns. Arginine facilitates elution of bound proteins from various column resins, including Protein-A or dye affinity columns and hydrophobic interaction columns. This review covers various biotechnology applications of amino acids, in particular arginine. Springer-Verlag, 2007 Keywords: Protein purification - Osmolyte - Formulation - Lyophilization - Aggregation suppression nationallicence Arakawa T. Alliance Protein Laboratories, Thousand Oaks, CA, USA aut Tsumoto K. Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, Japan aut Kita Y. Department of Pharmacology, KEIO University School of Medicine, Tokyo, Japan aut Chang B. Integrity Biosolution, Camarillo, CA, USA aut Ejima D. Amino Science Laboratories, Ajinomoto Co. Inc., Kawasaki, Kanagawa, Japan aut Amino Acids Springer-Verlag 33/4(2007-11-01), 587-605 0939-4451 33:4<587 2007 33 726 https://doi.org/10.1007/s00726-007-0506-3 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-007-0506-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Arakawa T. Alliance Protein Laboratories, Thousand Oaks, CA, USA aut NATIONALLICENCE 700 1- Tsumoto K. Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, Japan aut NATIONALLICENCE 700 1- Kita Y. Department of Pharmacology, KEIO University School of Medicine, Tokyo, Japan aut NATIONALLICENCE 700 1- Chang B. Integrity Biosolution, Camarillo, CA, USA aut NATIONALLICENCE 700 1- Ejima D. Amino Science Laboratories, Ajinomoto Co. Inc., Kawasaki, Kanagawa, Japan aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 33/4(2007-11-01), 587-605 0939-4451 33:4<587 2007 33 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer