Abstract
A putative SchistoFLRFamide receptor in CNS membrane preparations of Locusta migratoria was characterized by cold competition binding and kinetic binding assays using [ 125I][Y 1]SchistoFLRFamide ([ 125I]YDVDHVFLRFamide) as a radioligand. Binding to this site was saturable, specific, reversible, and of high-affinity. Data fit to a single-site binding model by non-linear regression (r 2 = 0.99) estimated K d = 1.73 ± 0.45 × 10 −9 M and B max = 49.0 ± 12.2 fmol · mg −1 tissue. Total binding of [ 125I][Y 1]SchistoFLRFamide to membrane preparations was reduced in the presence of GTPγS, an indication that the putative receptor is G protein-coupled. Structure-activity studies determined that the minimum sequence required for binding was HVFLRFamide. Other aspects of the ligand receptor interaction were also examined.
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