Identification and characterization of juvenile hormone affinity chromatography purified proteins

Juvenile hormone analog interacting proteins from Drosophila S2 cells were captured through affinity chromatography and then identified using mass spectrometry and peptide mass fingerprinting. Over 100 proteins, specifically bound to the stable JH analog column, were identified. Proteins were then characterized using the wealth of information from many Drosophila databases. Gene ontology analysis showed processes in agreement with the known actions of JH including development, reproduction and morphogenesis.