Glycyl betaine is effective in slowing down the irreversible denaturation of a detergent-solubilized membrane protein, sarcoplasmic reticulum Ca2+-ATPase (SERCA1a).
Many membrane proteins become labile when they are solubilized by detergent. Here we show that the presence of high concentrations of glycyl betaine stabilizes one of these proteins, the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a), solubilized with nonionic detergents like n-dodecyl beta-d-maltopyranoside (DDM) or octaethylene glycol monododecyl ether (C(12)E(8)) which are commonly used for its purification or crystallization. Betaine at high concentrations might become useful as a stabilizing agent for detergent-solubilized membrane proteins, for instance during purification procedures or during the long periods of time required for crystallogenesis.
Montigny
Cédric
C
CNRS, URA 2096, Systèmes Membranaires, Photobiologie, Stress et Détoxication, F-91191 Gif-sur-Yvette, France.
Arnou
Bertrand
B
Champeil
Philippe
P
D001622:Betaine / Q000494:pharmacology*; D003902:Detergents / Q000737:chemistry; D006801:Humans; D008320:Maltose / Q000031:analogs & derivatives / Q000737:chemistry; D011092:Polyethylene Glycols / Q000737:chemistry; D011489:Protein Denaturation / Q000187:drug effects; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases / Q000737:chemistry / Q000187:drug effects*; D012995:Solubility
D003902:Detergents; C411362:dodecyl maltopyranoside; C017272:dodecyloctaethyleneglycol monoether; D001622:Betaine; D011092:Polyethylene Glycols; D008320:Maltose; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases; C506943:ATP2A1 protein, human