Identification of a juvenile hormone binding protein in the castes of the termite,Reticulitermes flavipes,by photoaffinity labeling |
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| Institution: | 1. College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China;2. State & Local Joint Engineering Research Center of Green Pesticide Invention and Application, Jiangsu, China;1. Department of Molecular Biology and Biochemistry, University of California, Irvine, CA, USA;2. Department of Microbiology & Molecular Genetics, University of California, Irvine, CA, USA;1. College of Chemistry and Chemical Engineering, Zhengzhou Normal University, Zhengzhou 450044, China;2. College of Chemistry, Zhengzhou University, Zhengzhou 450001, China;3. New Materials Technology and Processing Research Center, Department of Chemistry, Neyshabur Branch, Islamic Azad University, Neyshabur, Iran;1. Graduate School of Science and Engineering, University of Toyama, Toyama, Japan;2. Tropical Biosphere Research Center, University of the Ryukyus, Nishihara, Japan;1. Department of Biology, University of Texas at San Antonio, San Antonio, TX, 78249, USA;2. USDA-ARS, Knipling-Bushland U.S. Livestock Insects Research Lab, Kerrville, TX, 78028, USA;3. Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, 78249, USA;4. USDA-ARS, San Joaquin Valley Agricultural Sciences Center, Parlier, CA, 93648, USA;5. Department of Neuroscience, Developmental and Regenerative Biology, University of Texas at San Antonio, San Antonio, TX, 78249, USA |
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| Abstract: | Hemolymph proteins of the Eastern subterranean termite, Reticulitermes flavipes (Isoptera, Rhinotermitidae, Rhinotermitinae) were examined from sterile and reproductive castes using native and denaturing polyacrylamide gel electrophoresis (PAGE). A high-mass protein (ca. 700 kDa) exhibited specific, JH III-displaceable photoaffinity labeling with 3H]EFDA, a diazoacetate analog of JH III. This protein was present in each termite caste, and had the characteristics of a glycosylated lipoprotein, i.e. a lipophorin. The JH-binding subunit of this protein showed a molecular size of 230 kDa using SDS-PAGE. The differences in the hemolymph proteins present in the soldiers, workers, larvae, nymphs, and replacement reproductives of this rhinotermitid are discussed. |
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