Back to Search
Start Over
Novel GTP-binding proteins in plasma membranes and zymogen granule membranes from rat pancreas and in pancreatic AR 4-2J cell membranes
- Source :
- FEBS letters, 271 (1-2
- Publication Year :
- 1990
-
Abstract
- Photoaffinity labeling with [α-32P]GTP allowed to detect a 54 kDa GTP-binding protein in rat pancreatic plasma membranes and in pancreatic AR 4-2J cell membranes. Like the 42 and 48 kDa G(s)α subunits and the 41 kDa G(i)α subunit, this protein was absent from zymogen granule membranes. Contrastingly, a new 28 kDa GTP-binding protein (detected by [α-32P]GTP binding on immobilized proteins) and a 25 kDa protein (ADP-ribosylated by botulinum toxin D) were found in all three membrane preparations. This is to our knowledge the first report on GTP-binding proteins in zymogen granule membranes.<br />SCOPUS: ar.j<br />info:eu-repo/semantics/published
- Subjects :
- GTP'
(Rat pancreatic acinar cell line AR 4-2J)
Biophysique
GTP-binding protein
Biochemistry
Cell Membrane -- metabolism
Structural Biology
Zymogen granule membrane
Membrane Proteins -- metabolism
Guanosine Triphosphate -- metabolism
Enzyme Precursors
Chemistry
Cytotoxins
rat pancreas
Rat pancreatic acinar cell line AR 4-2J
Membrane
Cross-Linking Reagents
Guanosine Triphosphate
Poly(ADP-ribose) Polymerases
Biologie
ADP-ribosylation
Cytotoxins -- pharmacology
G protein
Protein subunit
Biochimie
Biophysics
Cytoplasmic Granules
Cell Line
GTP-binding protein regulators
GTP-Binding Proteins
Genetics
Pancreas -- drug effects -- metabolism
Animals
Molecular Biology
Pancreas
(Rat pancreas)
Cytoplasmic Granules -- enzymology
Enzyme Precursors -- metabolism
Binding protein
Cross-Linking Reagents -- metabolism
Cell Membrane
Biologie moléculaire
Membrane Proteins
GTP-Binding Proteins -- metabolism
Cell Biology
Zymogen granule
Rats
Biologie cellulaire
Poly(ADP-ribose) Polymerases -- metabolism
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 271
- Issue :
- 1-2
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....12dcd94ecbbb4f5a52e0f45a00a8e764