Abstract
Antisera (AS/1-AS/6) to purified bovine retinal transducin, a guanine nucleotide-binding protein, were produced in 6 rabbits. Immunoblots showed that the antisera varied in their reactivity with the subunits of transducin; AS/1 reacted strongly with all 3 subunits, while the others reacted with only the β and/or γ subunits. Only AS/1 specifically immunoprecipitated the α subunit radiolabeled with non-covalently bound guanine nucleotides. Immunostaining of plasma membrane proteins from non-retinal tissues with AS-1 revealed a single protein (approx. 35 kDa), most likely representing the β subunit of the guanine nucleotide-binding proteins (Gs and gi associated with adenylate cyclase. Cerebral cortex showed the highest content of this protein. Antisera against transducin provide a highly specific and sensitive probe for quantitation of the β subunit of Gs and Gi.
Original language | English (US) |
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Pages (from-to) | 321-325 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 172 |
Issue number | 2 |
DOIs | |
State | Published - Jul 9 1984 |
Externally published | Yes |
Keywords
- Adenylate cyclase
- Guanine nucleotide-binding protein
- Retina
- Rod outer segment membrane
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology