A. Pomes et al., TARGET SIZE ANALYSIS OF AN AVERMECTIN BINDING-SITE FROM DROSOPHILA-MELANOGASTER, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1339(2), 1997, pp. 233-238
A high-affinity avermectin binding site from Drosophila melanogaster h
ead membranes was subjected to target size analysis by radiation inact
ivation in order to determine the functional unit size. Using the [H-3
]ivermectin binding assay to assess ligand binding activity, the targe
t 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 bind
ing is a monomer. The membrane-associated acetylcholinesterase present
in the Drosophila head membranes was also analyzed by radiation inact
ivation and served as a control. By monitoring enzymatic activity, the
functional unit size of the Drosophila acetylcholinesterase was deter
mined 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.