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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 27-38 
    ISSN: 0739-4462
    Keywords: hormone ; HPLC ; ovary ; antibody ; PAGE ; pulse-chase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Trypsin modulating oostatic factor (TMOF) was followed by RIA in the ovary of female Aedes aegypti before and after the blood meal. The amount of TMOF in a pair of ovaries from females fed sugar for 3 days or blood for 24 h was low (1.7 ng). Between 24 and 48 h after the blood meal the amount of TMOF in the ovaries rapidly increased and reached a peak of 104 ng at 48 h. The amount of TMOF in the head of a female A. aegypti was very low (0.05 to 0.1 ng) during sugar and blood feeding. Immunocytochemical methodology identified the follicular epithelium as the site of biosynthesis of TMOF in the ovary. Females ovariectomized and fed a blood meal continued to synthesize trypsin for 64 h, whereas intact controls stopped at 40 h, indicating that a factor from the ovary regulates trypsin biosynthesis. Ovaries incubated in vitro with [3H]proline synthesized [pro-3H]TMOF that was identified by HPLC and by anti-TMOF serum. The ovary started to synthesize TMOF in vitro 24 h after the blood meal, and the synthesis reached a peak at 36 h and then declined. The synthesis of TMOF by the ovary is closely correlated with the termination of trypsin biosynthesis in the female mosquito's midgut. Ovaries that were pulsed with [3H]proline for 30 min synthesized [pro-3H]TMOF which was chased into the medium with unlabeled proline, indicating that the hormone is secreted by the ovary. These results indicate that TMOF is a secretory peptide, synthesized by the ovarian follicular epithelium and that it modulates trypsin biosynthesis in the mosquito's gut. © 1994 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 16 (1991), S. 165-175 
    ISSN: 0739-4462
    Keywords: chemotaxonomy ; cuticular hydrocarbons ; gas-liquid chromatography ; identification ; peak ratios ; adults ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Comparison of the presence and quantities of cuticular hydrocarbons has been used successfully for identifying sibling species and races of several groups of insects. This approach has been extended to four species of moths previously regarded as belonging to the same genus, Heliothis. Gas chromatography was used to quantify the numerous high-molecular weight alkanes found on the cuticle of two pairs of closely related species: Helicoverpa zea and Helicoverpa armigera, and Heliothis virescens and Heliothis subflexa. Both sexes of H. zea and H. armigera contained different quantities of several alkanes that could be used for unambiguous identification. Similar comparisons of H. subflexa and H. virescens showed four peak ratios that were different for each species. Sexual dimorphism was minor in H. subflexa and H. virescens.
    Additional Material: 4 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 11-25 
    ISSN: 0739-4462
    Keywords: hormone ; HPLC ; gas chromatography ; tissue culture ; methoxyhydrin derivative ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Synthesis of (10R)-juvenile hormone III (JH III) outside the corpora allata (CA) was investigated in female Aedes aegypti. Intact females or ligated abdomens of blood-fed and sugar-fed females synthesized in vivo [12-3H]JH III-like molecules from [12-3H]-methyl farnesoate, indicating that an organ(s) in the female abdomen, other than the CA, converted methyl farnesoate into JH III. To find out the organ(s) that synthesized JH III-like molecules, ovaries, fat bodies, and midguts were incubated in vitro with [12-3H]methyl farnesoate and the synthesis of JH III-like molecules was compared with JH III synthesized by CA. To identify tissue(s) having both farnesoic acid methyl transferase and farnesoate epoxidase, enzymes that convert farnesoic acid into JH III, ovaries, and fat bodies were removed from sugar and blood-fed females and incubated with [12-3H]farnesoic acid. Chemical derivatization by methoxyhydrin formation followed by esterification with (+)-α-methoxy- α-trifluoromethyl phenylacetic (MTPA) acid chloride and reversed phase liquid chromatography identified (10R)-JH III methoxyhydrin (+)-MTPA ester as the sole JH III-like molecule produced in tissue culture incubation of ovaries. Since only (10R)-JH III is produced and not racemic JH III, the oxidation of farnesoic acid must be enzymatically mediated. Ovaries and corpora allata of female A. aegypti also synthesized [3H,14C]JH III from L-[methyl-3H]methionine and [14C]acetate which was characterized by HPLC and gas chromatography. These results suggest that mosquito ovary can synthesize (10R)-JH III from farnesoic acid, and that this tissue synthesizes JH III-like molecules from L-methionine and acetate. © 1994 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 23 (1993), S. 53-65 
    ISSN: 0739-4462
    Keywords: Anasterpha ; extract ; discriminant analysis ; alkanes ; gas-liquid chromatography ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Hydrocarbons extracted from seven species of tephritid fruit fly larvae were analyzed using capillary column gas-liquid chromatography and gas-liquid chromatography/mass spectrometry. Interspecific variation in hydrocarbon patterns was evaluated using both classical and nonparametric discriminant analysis for four of the seven Anastrepha taxa; A. acris, A. Fraterculus, A. suspensa and A. obliqua. Three of the four taxa, excluding A. acris, were correctly classified using a linear discriminant model at 72-83% and a nonparametric kernel density discriminant model at 87-92%. © 1993 Wiley-Liss. Inc.
    Additional Material: 1 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 21 (1992), S. 13-21 
    ISSN: 0739-4462
    Keywords: A. aegypti ; peptide hormone ; antibodies ; trypsinlike enzyme ; inhibition ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Trypsin modulating oostatic factor (TMOF), a decapeptide (H-YDPAPPPPPP-OH) that signals the termination of trypsinlike enzyme biosynthesis in the mosquito midgut, was covalently bound to Keyhole Limpet Hemocyanin using N-hydroxysuccinimide and dicyclohexylcarbodiimide. Polyclonal antibodies raised in rabbits against this conjugate were used to develop specific RIA and enzyme linked immunosorbent assay (ELISA) to detect the peptide hormone in female Aedes aegypti. TMOF and its analogs TMOF(B) (H-DYPAPPPPPP-OH), P4 (H-YDPAPPPP-OH), P1 (H-YDPAP-OH), and poly-L-proline were tested with the antiserum. The antiserum fully recognized TMOF and partially recognized P4. Using both RIA and ELISA, we report that the amount of TMOF in the mosquito ovary is 100 ± 20 ng (S.E.) and 96 ± 1.4 ng (S.E.), respectively, for each assay. Minute quantities of TMOF a thousandfold lower than in the ovary were found in the mosquito brain, indicating that the hormone is probably not neural but ovarian in origin. © 1992 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
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