| Title : Characterization of acetylcholinesterase activity from Drosophila melanogaster - Melanson_1985_Comp.Biochem.Physiol.C_81_87 |
| Author(s) : Melanson SW , Yun CH , Pezzementi ML , Pezzementi L |
| Ref : Comparative Biochemistry & Physiology C , 81 :87 , 1985 |
| Abstract : The acetylcholinesterase activity of the fruit fly, Drosophila melanogaster, was characterized biochemically. The activity is associated with a glycoprotein which is divided between a detergent-extractable membrane-bound fraction and a soluble fraction. The acetylcholinesterase activity is concentrated in the head of the insect. Through pharmacological methods, greater than 95% of the cholinesterase is judged to be true acetylcholinesterase, and not pseudocholinesterase. As expected for an acetylcholinesterase, the enzyme has a high affinity for acetylthiocholine and is inhibited by excess concentrations of acetylthiocholine. The soluble enzyme is found predominantly as a 7.8 S form; a smaller amount of an approximately 6 S form is also present, and a greater than or equal to 14 S form may exist. The detergent-solubilized acetylcholinesterase has a sedimentation coefficient of 7.5 S in the presence of detergent. The thermal inactivation rates for the soluble and the membrane bound enzymes are markedly different. |
| ESTHER : Melanson_1985_Comp.Biochem.Physiol.C_81_87 |
| PubMedSearch : Melanson_1985_Comp.Biochem.Physiol.C_81_87 |
| PubMedID: 2861064 |
Melanson SW, Yun CH, Pezzementi ML, Pezzementi L (1985)
Characterization of acetylcholinesterase activity from Drosophila melanogaster
Comparative Biochemistry & Physiology C
81 :87
Melanson SW, Yun CH, Pezzementi ML, Pezzementi L (1985)
Comparative Biochemistry & Physiology C
81 :87