1. Degradation of pheromone biosynthesis-activating neuropeptide (PBAN) by hemolymph enzymes of the tobacco hornworm,Manduca sexta, and the corn earworm,Helicoverpa zea
- Author
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Gunter F. Weirich, Ashok K. Raina, Edward P. Masler, Mark F. Feldlaufer, Jan Kochansky, James A. Svoboda, and William R. Lusby
- Subjects
medicine.medical_specialty ,animal structures ,Molecular Sequence Data ,Moths ,Pheromones ,Cellular and Molecular Neuroscience ,chemistry.chemical_compound ,Amastatin ,Hemolymph ,Manduca ,Internal medicine ,Endopeptidases ,medicine ,Animals ,Protease Inhibitors ,Amino Acid Sequence ,Molecular Biology ,Pharmacology ,chemistry.chemical_classification ,biology ,Neuropeptides ,fungi ,Leupeptin ,Cell Biology ,biology.organism_classification ,EGTA ,Enzyme ,Endocrinology ,chemistry ,Biochemistry ,Manduca sexta ,Pheromone biosynthesis activating neuropeptide ,Molecular Medicine ,Female ,Helicoverpa zea - Abstract
The tritium-labeled bis-norleucine analog of Helicoverpa zea pheromone biosynthesis-activating neuropeptide ([3H]NLPBAN) was incubated in vitro with hemolymph from Manduca sexta or H. zea adult females. The incubations resulted in the formation of several tritium-labeled degradation products. At a [3H]NLPBAN concentration of 0.9 microM the degradation proceeded at a very slow but physiologically plausible rate (2-10 fmol/min/microliters hemolymph). The primary [3H]NLPBAN degradation reaction in M. sexta hemolymph was not inhibited by 20 microM 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 of M. sexta and H. zea contains peptidase(s) capable of inactivating circulating PBAN.
- Published
- 1995
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