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) |
|---|---|
| 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
Fingerprint
Dive into the research topics of 'GTP-Binding proteins in brain and neutrophil are tethered to the plasma membrane via their amino termini'. Together they form a unique fingerprint.Cite this
- APA
- Standard
- Harvard
- Vancouver
- Author
- BIBTEX
- RIS