Functional heterogeneity of transducin α subunits
- 6 February 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 422 (3), 343-345
- https://doi.org/10.1016/s0014-5793(98)00037-4
Abstract
The N-terminal glycine of transducin α subunits is acylated by lauroyl (C12:0), myristoyl (C14:0), (cis-Δ5)-tetradecaenoyl (C14:1) or (cis,cis-Δ5,Δ8)-tetradecadienoyl (C14:2) fatty acyl groups. We examined functional heterogeneity of transducin by sequentially eluting it from bleached outer segments using increasing concentrations of GTP then identifying the N-terminal acyl groups on the eluted α subunits. C14:2 acylated transducin eluted at low GTP concentrations followed by C12:0, C14:1 and C14:0 transducin at higher GTP concentrations. This suggests functional heterogeneity in the different forms of transducin α subunitsKeywords
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