Degradation of pheromone biosynthesis-activating neuropeptide (PBAN) by hemolymph enzymes of the tobacco hornworm,Manduca sexta,and the corn earworm,Helicoverpa zea |
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Authors: | G F Weirich J P Kochansky E P Masler W R Lusby M F Feldlaufer A K Raina J A Svoboda |
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Institution: | 1. Insect Neurobiology and Hormone Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Bldg. 467, BARC-East, 10300 Baltimore Ave., 20705-2350, Beltsville, Maryland, USA
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Abstract: | The tritium-labeled bis-norleucine analog ofHelicoverpa zea pheromone biosynthesis-activating neuropeptide (3H]NLPBAN) was incubated in vitro with hemolymph fromManduca sexta orH. zea adult females. The incubations resulted in the formation of several tritium-labeled degradation products. At a 3H]NLPBAN concentration of 0.9 μM the degradation proceeded at a very slow but physiologically plausible rate (2–10 fmol/min/μl hemolymph). The primary 3H]NLPBAN degradation reaction inM. sexta hemolymph was not inhibited by 20 μM leupeptin, 0.1 mM amastatin, 1 mM EDTA, 1 mM EGTA, 1 mM 1,10-phenanthroline, or 2 mM 4-(2-aminoethyl)benzenesulfonyl fluoride; but secondary reactions may have been affected, as some of the inhibitors changed the radio-HPLC profile of the degradation products. It is concluded that hemolymph ofM. sexta andH. zea contains peptidase(s) capable of inactivating circulating PBAN. |
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