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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (5)
  • Schistocerca nitens  (1)
  • 1
    Electronic Resource
    Electronic Resource
    JH III levels in larvae and pharate pupae of Anastrepha suspensa (Diptera: Tephritidae) and in larvae of the parasitic wasp Biosteres longicaudatus (Hymenoptera: Braconidae) (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 13 (1990), S. 53-62 
    Details
    ISSN: 0739-4462
    Keywords: Caribbean fruit fly ; juvenile hormone ; JH esterase ; superparasitism ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: This is the first report of a juvenile hormone (JH) in the Caribbean fruit fly, Anastrepha suspensa (Diptera: Tephritidae). JH III was identified in whole body extracts of L3 (final instar) larvae and pharate pupae (PhP) by using a physicochemical method. JH III was also found in PhP superparasitized (up to 11.3 ± 3.5 S.D. parasites/host) by the solitary wasp Biosteres longicaudatus (Hymenoptera: Braconidae) and in first instars of the parasite. The levels of JH III in hosts were up to 15 × higher than those of the controls. The JH esterase (JHE) levels in the hemolymph of 1-day-old PhP controls were significantly (P 〈 0.05) higher than those of superparasitized individuals. These results suggest that the elevated JH III levels induced by superparasitism may arise from JH buildup due either to decreased JHE activity to continued synthesis of JH by the ring gland or to secretion of JH III by the parasites into the host's hemocoel.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940130106
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of the juvenile hormone epoxide hydrolase (JHEH) and juvenile hormone diol phosphotransferase (JHDPT) from Manduca sexta Malpighian tubules (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 30 (1995), S. 255-270 
    Details
    ISSN: 0739-4462
    Keywords: juvenile hormone kinase ; tritiation ; HPLC ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Juvenile hormone epoxide hydrolase (JHEH) and juvenile hormone diol phosphotransferase (JHDPT) were characterized from the Malpighian tubules of day 1 fifth instar Manduca sexta. An improved RP-HPLC assay is described for the major metabolites of (10R, 11S) juvenile hormone I: diol, acid, aciddiol, and diol-phosphate. JHEH is strictly associated with membrane fractions, while JHDPT is cytosolic. JHEH may be solubilized in active form by the nonionic detergents Thesit or MEGA-8. Separation of Malpighian tubule cytosol proteins using preparative isoelectric focusing yields two zones which contain JHDPT activity, at pl 4.8-5.1 and 6.8-8.2. The partially purified JHDPT from either zone requires both ATP and Mg2+ for activity, so this enzyme may be formally called either ATP:juvenile hormone diol phosphotransferase or juvenile hormone diol kinase (EC 2.1.7.3.). Metabolites more polar than JH I aciddiol and JH I diol-phosphate are generated in vivo from either [3H]JH I or [3H]JH I diol. © 1995 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940300213
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  • 3
    Electronic Resource
    Electronic Resource
    Comparative metabolism of isoleucine by corpora allata of nonlepidopteran insects versus lepidopteran insects, in relation to juvenile hormone biosynthesis (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 19 (1992), S. 1-15 
    Details
    ISSN: 0739-4462
    Keywords: branched-chain amino acid ; 2-keto-3-methylvalerate ; 2-methylbutyrate ; propionate ; acetate ; Manduca sexta ; Hyalophora cecropia ; Samia cynthia ; Peiplaneta americana ; Schistocerca nitens ; Tenebrio molitor ; Diploptera punctata ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We studied the metabolism of [U-14C]isoleucine by intact and homogenized corpora allata (CA) from various insect species to determine how this substrate is converted to precursors of juvenile hormone (JH). CA homogenates of the lepidopterans Manduca sexta, Hyalophora cecropia, and Samia cynthia metabolize [U-14C]isoleucine to several products including 2-keto-3-methyl-valerate, 2-methylbutyrate, CO2, propionate, and acetate. Intact CA of male H. cecropia produce particularly high levels of 2-keto-3-methylvalerate, indicating a highly active branched-chain-amino acid transaminase. In contrast, CA homogenates from the nonlepidopterans Periplaneta americana, Schistocerca nitens, Tenebrio molitor, and Diploptera punctata barely metabolize [U-14C]isoleucine. However, P. americana CA homogenate metabolizes [U-14C]2-keto-3-methylvalerate, the transamination product of [U-14C]isoleucine, more rapidly than does a homogenate of M. sexta CA. Furthermore, intact CA from P. americana incubated with [U-14C]2-keto-3-methylvalerate incorporate low levels of 14C into JH III, but do not metabolize this substrate to JH II or JH I. Intact CA from female Diploptera punctata produce very high levels of JH III, but are also unable to incorporate radiolabel from [U-14C]isoleucine into JH III, which substantiates our findings with other nonlepidopteran CA. The results suggest that CA of nonlepidopteran insects lack an active branched-chain amino acid transaminase and, consequently, are unable to utilize these substrates for JH biosynthesis.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940190102
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation of two arginine vasopressin-like factors from ganglia of Locusta migratoria (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 5 (1987), S. 157-166 
    Details
    ISSN: 0739-4462
    Keywords: diuretic hormone ; reversed-phase liquid chromatography ; migratory locust ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Tissues of Locusta migratoria are known to contain a material which crossreacts with an antibody against arginine vasopressin (AVP), and this factor has been correlated with the diuretic hormone of this species. In this paper, we report the isolation of two AVP-like factors from suboesophageal ganglia and thoracic ganglia of Locusta migratoria. The less abundant, more hydrophobic of these AVP-like factors shows diuretic activity in an assay where excretion of amaranth dye from Locusta migratoria hemolymph is used as the scoring criterion. After extracting a total of ∼ 51,000 ganglia with an acidic solvent, the crude extract was prepurified by batch adsorption/elution from disposable reversed-phase cartridges. The prepurified extract was then sequentially purified by reversed-phase liquid chromatography using solvent programs of substantially differing selectivity. The more abundant factor was isolated to apparent homogeneity in three steps, while the less abundant factor required four or five steps. Use of a C4 reversed-phase column minimized losses of the minor, more hydrophobic factor.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940050302
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  • 5
    Electronic Resource
    Electronic Resource
    Characteristics of Locusta migratoria diuretic hormone (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 133-140 
    Details
    ISSN: 0739-4462
    Keywords: corpora cardiaca ; cAMP ; CRF ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Locusta migratoria diuretic hormone (Lom-DH) is a linear 46 amino acid peptide, amidated at the C-terminus. The purified native hormone and synthetic peptide similarly stimulate the secretion of cAMP by isolated Malpighian tubules in vitro in a dose-dependent manner. The degree of stimulated fluid secretion in the isolated Malpighian tubule assay is similar for the native and synthetic hormone. Based on ELISA assay, Lom-DH is mainly found in the storage lobes of the corpora cardiaca (∼ 12 pmol per gland pair) and to a small extent in the brain. Marginal amounts can be detected in the hemolymph. No detectable amounts were found in the glandular lobes of the corpora cardiaca or in the corpora allata or subesophageal ganglion. © 1993 Wiley-Liss, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940220111
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