ArticleThe protein journal2010
Ternary system of solution additives with arginine and salt for refolding of beta-galactosidase.
Article in The protein journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 11 citations in OpenAlex.
- Enhancing the Yield of Active Recombinant Chitobiase by Physico-Chemical and In Vitro Refolding Studies.The protein journal · 2016Article
- Article
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3 authors at 1 institution in 1 country.
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Abstract
(L)-Arginine hydrochloride (Arg HCl) has been used for protein refolding as a universal aggregation suppressor for monomeric proteins. This paper presents an investigation of the refolding of tetrameric beta-galactosidase (beta-gal) using Arg HCl and other salts. In a binary system using only Arg HCl, the refolding yield of beta-gal increased with increasing concentration up to 0.2 M. However, the refolding yield sharply decreased above this concentration, reaching the level below the control yield of 5% at 0.5 M and near zero above 0.75 M, an observation unexpected from monomeric proteins. In a ternary system using both 0.2 M Arg HCl and another salt, the refolding yield increased up to 1.5-fold higher than that in the binary system. These data indicate that aggregation suppressive effects of protein increase with Arg HCl concentration, but also are deleterious to self-association of the protein. This dual nature of Arg HCl effects may have to be taken into account in its application for refolding of oligomeric proteins.
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