Value of heptyl-beta-D-thioglucoside, a new nonionic detergent, in studies on membrane proteins.
A new nonionic detergent, heptylthioglucoside, was synthesized and found to be more soluble than octylthioglucoside in water at low temperatures. Use of this detergent for solubilization and reconstitution of membrane proteins of Escherichia coli was examined. Heptylthioglucoside was as effective as octylthioglucoside and octylglucoside in solubilizing membrane proteins, and by the heptylthioglucoside-dilution procedure the H+-translocating ATPase (F1F0) and melibiose carrier could easily be reconstituted into liposomes. It is concluded that heptylthioglucoside is very useful in studies on membrane proteins.
Shimamoto
T
T
Saito
S
S
Tsuchiya
T
T
D001426:Bacterial Proteins / Q000302:isolation & purification; D055598:Chemical Phenomena; D002621:Chemistry; D003902:Detergents; D004926:Escherichia coli / Q000032:analysis; D008565:Membrane Proteins / Q000302:isolation & purification*; D026901:Membrane Transport Proteins / Q000302:isolation & purification; D006180:Proton-Translocating ATPases / Q000302:isolation & purification; D012995:Solubility; D013501:Surface-Active Agents; D027981:Symporters; D013696:Temperature; D013865:Thioglycosides
D001426:Bacterial Proteins; D003902:Detergents; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D013501:Surface-Active Agents; D027981:Symporters; D013865:Thioglycosides; C046542:heptyl 1-thioglucoside; C021548:melibiose permease; D006180:Proton-Translocating ATPases