GTP-Binding Protein Fragment, G alpha

- Overview
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    Background
    
    Sequence: Cys-Gly-Ala-Gly-Glu-Ser-Gly-Lys-Ser-Thr-Ile-Val-Lys-Gln-Met-Lys
    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
- Properties
  - Categories
    
    Hydrolyzes GTP to GDP
    
    Alternative Name
    
    H2N-Cys-Gly-Ala-Gly-Glu-Ser-Gly-Lys-Ser-Thr-Ile-Val-Lys-Gln-Met-Lys-OH
    
    Molecular Formula
    
    C66H118N20O23S2
    
    Molecular Weight
    
    1623.89
    
    Appearance
    
    A solid
    
    Purity
    
    74.64%
    
    Solubility
    
    insoluble in EtOH; ≥162.3 mg/mL in DMSO; ≥51.5 mg/mL in H2O
    
    Storage
    
    Store at -20°C
    
    * For Research Use Only