|GTP-Binding Protein Fragment, G alphaHydrolyzes GTP to GDP|
Sample solution is provided at 25 µL, 10mM.
Publications citing ApexBio Products
|Cas No.||SDF||Download SDF|
|Solubility||Storage||Store at -20°C|
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 (composed of all but an amino-terminal 2kDa piece) from the membrane. Previous results indicated that alpha subunits are essentially cytoplasmic proteins tethered to the inner surface of the membrane via an amino terminal stalk.
1. Brock Eide, Peter Gierschik, Graeme Milligan, Ian Mullaney, Cecilia Unson, Paul Goldsmith, Allen Spiegel, Biochemical and Biophysical Research Communications, Volume 148, Issue 3, 13 November 1987, Pages 1398–1405
2. J. Falloon, H. Malech, G. Milligan, C. Unson, R. Kahn, P. Goldsmith, A. Spiegel, FEBS Letters, 209 (1986), pp. 352–356