Isolation and solubilization of cellular membrane proteins from bacteria.
Membrane proteins are rarely identified in two-dimensional electrophoretic (2-DE) proteomics maps. This is because of low abundance, poor solubility, and inherent hydrophobicity. In this study, membrane preparations from the Gram-positive bacterium Streptococcus mutans were isolated from protoplasts and by mechanical grinding. Membrane proteins were extracted using a mixture of trifluroethanol and chloroform, solubilized using highly chaotropic buffer containing ASB-14 and Triton X-100 and subjected to two-dimensional gel electrophoresis.
Zuobi-Hasona
Kheir
K
University of Florida, Gainesville, Florida, USA.
Brady
L Jeannine
LJ
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D015180:Electrophoresis, Gel, Two-Dimensional; D008565:Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification*; D012995:Solubility; D013295:Streptococcus mutans / Q000737:chemistry*
D001426:Bacterial Proteins; D008565:Membrane Proteins