Properties of achetakinin binding sites on Malpighian tubule membranes from the house cricket, Acheta domesticus

@article{Chung1995PropertiesOA,
  title={Properties of achetakinin binding sites on Malpighian tubule membranes from the house cricket, Acheta domesticus},
  author={Jum Sook Chung and Colin H. Wheeler and Graham John Goldsworthy and Geoffrey M. Coast},
  journal={Peptides},
  year={1995},
  volume={16},
  pages={375-382}
}
A biologically active 125I-labeled analogue of AK-II (3'-hydroxyphenyl propionic-Gly-Gly-Gly-Phe-Ser-Pro-Trp-Gly-NH2) was used to investigate the properties of achetakinin binding sites on plasma membranes from Malpighian tubules of Acheta domesticus. With optimized conditions, binding was rapid, reversible, and specific, and saturation studies revealed a single class of binding sites with Kd 0.55 nM and Bmax 39.9 fmol/mg membrane protein. The affinities of achetakinins for binding sites on… CONTINUE READING