title: Suppression of protein aggregation by L-arginine.
abstract: L-Arginine is one of the most commonly used and most generally applicable suppressors of protein aggregation. Its effect as enhancer of in vitro protein refolding was serendipitously discovered two decades ago. This article aims at giving a brief overview about the discovery of the arginine effect, the range of its applications that have been explored over the past two decades, and of the current state of the discussion regarding the mechanisms responsible for the action of L-arginine as suppressor of aggregation.
authors.affiliation: Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Saale, Germany. christian.lange@biochemtech-uni-halle.de
authors.forename: Christian
authors.initials: C
authors.lastname: Lange
authors.forename: Rainer
authors.initials: R
authors.lastname: Rudolph
mesh_terms: D001120:Arginine / Q000737:chemistry*; D001702:Biopharmaceutics / Q000379:methods*; D005591:Chemical Fractionation / Q000379:methods; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000302:isolation & purification*; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D013678:Technology, Pharmaceutical / Q000379:methods*
chemical_list: D046912:Multiprotein Complexes; D011506:Proteins; D001120:Arginine