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Review: Why is Arginine Effective in Suppressing Aggregation?

[ Vol. 12 , Issue. 7 ]

Author(s):

Kohei Tsumoto, Daisuke Ejima, Yoshiko Kita and Tsutomu Arakawa   Pages 613 - 619 ( 7 )

Abstract:


Arginine is finding a wide range of applications in production of proteins. Arginine has been used for many years to assist protein refolding. This effect was ascribed to aggregation suppression by arginine of folding intermediates during protein refolding. Recently, we have observed that arginine facilitates elution of antibodies during Protein-A chromatography and solubilizes insoluble proteins from inclusion bodies, which both can be ascribed to weakening of protein-protein interactions. In order to gain understanding on why arginine is effective in reducing protein-protein interactions and suppressing aggregation, the effects of arginine on stability and solubility of pure proteins have been examined, which showed that arginine is not a protein-stabilizer, but is an aggregation suppressor. However, there is no explanation proposed so far on why arginine suppresses aggregation of proteins. This review addresses such question and then attempts to show differences between arginine and strong denaturants, which are also known as an aggregation suppressor.

Keywords:

Arginine, Protein-A, protein-protein interactions, chromatography

Affiliation:

Alliance ProteinLaboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, USA;



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