Paper Report for: Pomes_1997_Biochim.Biophys.Acta_1339_233
Reference
Title: Target size analysis of an avermectin binding site from Drosophila melanogaster Pomes A, Kempner E, Rohrer S Ref: Biochimica & Biophysica Acta, 1339:233, 1997 : PubMed
A high-affinity avermectin binding site from Drosophila melanogaster head membranes was subjected to target size analysis by radiation inactivation in order to determine the functional unit size. Using the [3H]ivermectin binding assay to assess ligand binding activity, the target size was determined to be 44.3 +/- 3.9 kDa. This result suggests that the size of the functional unit required for high-affinity ligand binding is a monomer. The membrane-associated acetylcholinesterase present in the Drosophila head membranes was also analyzed by radiation inactivation and served as a control. By monitoring enzymatic activity, the functional unit size of the Drosophila acetylcholinesterase was determined to be 70 +/- 9.7 kDa. This corresponds to the molecular weight of a dimer composed of a 55 kDa subunit and a 16-18 kDa subunit.
        
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Pomes A, Kempner E, Rohrer S (1997) Target size analysis of an avermectin binding site from Drosophila melanogaster Biochimica & Biophysica Acta1339: 233-8
Pomes A, Kempner E, Rohrer S (1997) Biochimica & Biophysica Acta1339: 233-8