Abstract
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) |
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Pages (from-to) | 568-575 |
Number of pages | 8 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 129 |
Issue number | 2 |
DOIs | |
State | Published - Jun 14 1985 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology