In hydra the neuropeptide head activator (HA) is responsible for head-specific growth and differentiation processes. The effects of HA are mediated by high and low affinity receptors on hydra cells. In the current study HA receptors from a multi-headed mutant of Chlorohydra viridissima were solubilized from the membrane fraction using 1% Triton X-100 and 2.5 M urea. Scatchard analysis showed that the solubilized receptor had a Kd of 1.55 × 10-9 M, indicating the low affinity subtype of the HA receptor. The solubilized receptor was purified by DMAE chromatography and subsequent affinity chromatography to homogeneity. SDS-PAGE revealed a single protein band with a molecular mass of 96 ± 4 kDa. The native receptor eluted during gel filtration as a 113 kDa protein, and focussed with an isoelectric point of 4.8. © 1993.
Christians, S., Neubauer, K. H., & Ulrich, H. (1993). Purification and characterization of the head-activator receptor from a multi-headed mutant of chlorohydra viridissima. FEBS Letters, 316(2), 141–146. https://doi.org/10.1016/0014-5793(93)81203-C