Membrane protein solubilized by octyl-β-D-glucopyranoside in the presence of dispersed phospholipid was incubated with bath-sonicated liposomes and additional detergent. The proteoliposomes formed on dilution showed transport and exchange properties consistent with a reconstitution of phosphate: sugar 6-phosphate antiport. Thus, phosphate self-exchange was found only when protein from induced cells was used; this exchange was blocked by a sugar 6-phosphate, not by a sugar 1-phosphate; and proteoliposomes supported an accumulation of 2-deoxyglucose 6-phosphate with no added source of energy. Solubilization and reconstitution of protein was most effective when performed in the presence of gram-positive phospholipids.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jun 14 1985|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology