SUBCELLULAR LOCALIZATION AND PROPERTIES OF A CHOLINERGIC RECEPTOR ISOLATED FROM HOUSEFLY HEADS

@article{Donnellan1975SUBCELLULARLA,
  title={SUBCELLULAR LOCALIZATION AND PROPERTIES OF A CHOLINERGIC RECEPTOR ISOLATED FROM HOUSEFLY HEADS},
  author={John F. Donnellan and P. J. Jewess and Kenneth J. Cattell},
  journal={Journal of Neurochemistry},
  year={1975},
  volume={25}
}
—Protein(s) possessing the ligand‐binding properties expected of the insect cholinergic receptor were demonstrated in both aqueous and chloroform‐methanol extracts of an 80,000 g supernatant obtained from frozen housefly heads. There is reasonable correlation in both the properties and concentration of the housefly head cholinergic receptor in these radically different extracts. 
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ISOLATION AND PURIFICATION OF CHOLINERGIC RECEPTOR PROTEOLIPIDS FROM RAT GASTROCNEMIUS TISSUE 1
  • R. F. Taylor
  • Biology, Chemistry
    Journal of neurochemistry
  • 1978
TLDR
The purified receptor proteolipid resulting from wet tissue extraction has been characterized as a somatic, nicotinic cholinergic receptor by its specificity and binding kinetics toward a variety of drugs and toxins.
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References

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Purification of a Cholinergic Receptor Isolated from Housefly Heads
TLDR
The localization in a similar housefly head fraction (an 80000g supernatant) of a receptor-like material that binds with high affinity a number of cholinergic ligands such as acetylcholine, nicotine, atropine and decamethonium is reported.
BINDING OF MUSCARONE BY EXTRACTS OF HOUSEFLY BRAIN: RELATIONSHIP TO RECEPTORS FOR ACETYLCHOLINE
TLDR
The supernatant fluid fraction isolated from a homogenate of heads of houseflies bound muscarone reversibly, with a binding constant of 2·4 × 10−6m and an amount of 70 nmol/g of protein, suggesting both nicotinic and muscarinic characteristics in the mode of binding.
The isolation of an acetylcholine- and decamethonium-binding protein from housefly heads.
TLDR
Experiments are described showing that a proteolipid fraction with similar properties to those of the 'acetylcholine-receptor proteolIPids' described by De Robertis and his co-workers can be isolated from insect nervous tissue.
Isolation of a cholinergic proteolipid receptor from electric tissue.
A proteolipid protein having a high affinity for methyl (14)C-hexamethonium, (3)H-p-(trimethylammonium)-benzene diazonium fluoroborate, and (acetyl-1-(14)C)choline chloride was isolated and purified
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