| Autor: |
D N, Orlov, A R, Nezvetskiĭ, T G, Orlova, O V, Petrukhin, N Ia, Orlov |
| Rok vydání: |
2015 |
| Předmět: |
|
| Zdroj: |
Biofizika. 59(5) |
| ISSN: |
0006-3029 |
| Popis: |
The supposition that nucleoside diphosphate kinase is the enzyme that phosphorylates transducin beta-subunits on one of the histidine residues (His-266) has been analyzed. It stands the reason that 1) this enzyme is multifunctional and plays in particular the role of protein histidine kinase; and 2) the phosphorylated beta-subunit of transducin may activate transducin via the mechanism of transphosphorylation. Nevertheless, in our experiments, in which different forms of transducin preparations were incubated with α- and β-isoforms of recombinant rat NDP kinase in the presence of [γ32P]ATP or [γ32P]GTP (specific activity of about 1 Ci/mmol) followed by separation of proteins by electrophoresis and-gel radio-autography, the phosphorylation of the transducin beta-subunit wasn't succeeded to be found. The negative result of our experiments most likely implies that the major part of transducin beta-subunits in the preparations has already been phosphorylated via a process that takes place in vivo. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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