Treatment with crystalline ultra-pure urea reduces the aggregation of integral membrane proteins without inhibiting N-terminal sequencing.
Soulié S, Denoroy L, Le Caer JP, Hamasaki N, Groves JD, le Maire M.
Soulié S, et al. Among authors: le maire m, le caer jp.
J Biochem. 1998 Aug;124(2):417-20. doi: 10.1093/oxfordjournals.jbchem.a022128.
J Biochem. 1998.
PMID: 9685735
Free article.
These observations are useful for the study of integral membrane proteins, in particular to study their topology from proteolysis experiments, since heating in the presence of urea before SDS-PAGE reduces membrane protein aggregation [Soulie, S., Mo/ller, J.V., Falson, P., and …
These observations are useful for the study of integral membrane proteins, in particular to study their topology from proteolysis experiment …