Abstract
Using specific antisera raised against synthetic peptides, we find that three distinct GTP-binding protein alpha subunits remain bound to the plasma membrane even after activation with nonhydrolyzable GTP analog. Trypsin cleaves each alpha subunit at a site near the amino-terminus, and quantitatively releases the large fragment (comprising all but an amino-terminal 2kDa piece) from the membrane. Our results indicate that alpha subunits are essentially cytoplasmic proteins tethered to the inner surface of the membrane via an amino terminal stalk.
Original language | English (US) |
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Pages (from-to) | 1398-1405 |
Number of pages | 8 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 148 |
Issue number | 3 |
DOIs | |
State | Published - Nov 13 1987 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology