EFFECT OF SOLUBILIZATION ON THE BINDING-ACTIVITY OF A G-PROTEIN FROM THE MANDIBULAR ORGAN OF THE LOBSTER HOMARUS-AMERICANUS (NEPHROPIDAE, DECAPODA)

The binding of [S-35]GTP gamma S by the G-protein from the lobster man dibular organ was not affected by biogenic amines, synthetic eyestalk peptides or an extract of the X-organ-sinus gland complex from the eye stalk. This suggests that the G-protein is not part of the receptor ap paratus that controls the inhibition of methyl farnesoate synthesis. T he G-protein is deactivated during extraction from the membrane by the anionic detergents sodium cholate and SDS but may be solubilized usin g the nonionic detergents Triton X-100, Lubrol PX or Nonidet P-40.