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A juvenile hormone binding protein from the house fly and its possible relationship to insecticide resistance
Author(s) -
Plapp Frederick W.,
Cariño Flerida A.,
Wei Victor K.
Publication year - 1998
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1998)37:1<64::aid-arch8>3.0.co;2-v
Subject(s) - juvenile hormone , biology , biochemistry , binding protein , phormia regina , larva , gene , hormone , botany , calliphoridae
High‐affinity juvenile hormone 1 (JH) binding to protein was demonstrated in house fly adults and larvae. Techniques were developed to optimize isolation of the protein and measurement of binding kinetics. Resistant flies showed a significant decrease in JH affinity and a significant increase in JH binding site numbers compared to susceptibles. Genetic tests showed these changes mapped to chromosomes 5 and 2, respectively, the chromosomes that play a major role in metabolic resistance to insecticides. With larvae, purification of the binding protein was achieved with photolysis in combination with ammonium sulfate fractionation of cytosols. The purified protein had a molecular weight of ca. 22 kDa and occurred as a dimer. The 12 N‐terminal amino acids were identified. Possible relationships of JH binding proteins and metabolic resistance to insecticides are discussed. Arch. Insect Biochem. Physiol. 37:64–72, 1998. © 1998 Wiley‐Liss, Inc.