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Effect of solubilization on the binding activity of a G-protein from the mandibular organ of the lobster Homarus americanus (Nephropidae, Decapoda)

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, ISSN: 1096-4959, Vol: 112, Issue: 2, Page: 205-208
1995
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  • Citations
    1
    • Citation Indexes
      1
      • CrossRef
        1
  • Captures
    5

Article Description

The binding of [ 35 SIGTPγS by the G-protein from the lobster mandibular organ was not affected by biogenic amines, synthetic eyestalk peptides or an extract of the X-organ-sinus gland complex from the eyestalk. This suggests that the G-protein is not part of the receptor apparatus that controls the inhibition of methyl farnesoate synthesis. The G-protein is deactivated during extraction from the membrane by the anionic detergents sodium cholate and SDS but may be solubilized using the nonionic detergents Triton X-100, Lubrol PX or Nonidet P-40.

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