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  • 1
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Entomology 26 (1981), S. 1-28 
    ISSN: 0066-4170
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 37 (1981), S. 909-910 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary JH titers in the hemolymph of nymphal and adult femaleLocusta migratoria migratorioides (R. and F.) were determined using a selective mass spectrosc opic detection technique. Only JH III could be found in either stage, with no detectable JH I (or II). Titers observed were 10–1000-fold lower than those found via a recently reported radioimmunoassay procedure.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 42 (1986), S. 834-836 
    ISSN: 1420-9071
    Keywords: Juvenile hormone binding protein ; lipophorin ; juvenile hormone I ; juvenile hormone III
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Using two independent techniques, ultracentrifugation in a KBr-gradient, and native pore polyacrylamide gel electrophoresis in combination with [3H]-epoxyfarnesyldiazoacetate photoaffinity labeling, we showed that in the hemolymph ofPeriplaneta americana, and probably also inLeptinotarsa decemlineata JH-III binds to the lipophorin, whereas inLocusta migratoria JH-III binds to a different protein.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 43 (1987), S. 904-905 
    ISSN: 1420-9071
    Keywords: Juvenile hormone III ; hormone binding protein ; lipophorin ; enantioselectivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Binding specificity of juvenile hormone (JH) III enantiomers and analogs to hemolymph proteins ofLeptinotarsa decemlineata andLocusta migratoria was investigated by competitive displacement tests. The order of binding affinity was 10R-JH-III〉10R, 10S-JH-III≫10S JH-III〉 methylfarnesoate for analogs of the epoxide group and diazo-JHA-IV〉EFDA for analogs of the methylester. Both the epoxide and ester groups are important for the interaction of JH-III with its binding protein.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 43 (1987), S. 312-314 
    ISSN: 1420-9071
    Keywords: locust ; corpora allata ; JHBP ; hemolymph protein content ; hemolymph volume
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Hemolymph from adult femaleLocusta migratoria migratorioides was analyzed for binding of juvenile hormone III (JH-III) after allatectomy and transection of thenervus corporis allati 1 (NCA-I). These operations did not affect the apparent dissociation constant of the binding (Kd=3.3 10−8 M). The concentration of binding sites exhibited fluctuations in relation to age and type of operation: an increased concentration of binding sites in females with disconnected corpora allata and a decreased concentration in allatectomized females. The changes in concentration of binding sites was not due to differences in water content or hemolymph volume in operated animals. The hemolymph protein concentration was reduced after NCA-I transection and even more after allatectomy. However, variations in protein concentration did not correlate with changes in concentration of JH-III binding sites. The changes in binding site concentration were related to changes in JH-titer.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 45 (1989), S. 327-330 
    ISSN: 1420-9071
    Keywords: Carboxylesterase ; juvenile hormone esterase ; juvenile hormone binding protein ; hemolymph proteins ; migratory locust
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The main carboxylesterase in the hemolymph of the migratory locust,Locusta migratoria, is a protein of high molecular weight; about 700–750 kDa. This esterase hydrolyzes juvenile hormone III, α-naphthylacetate and β-naphthylacetate. The carboxylesterase dissociates to give an esterase of molecular weight 148 kDa after treatment of the hemolymph with mercaptoethanol.
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  • 7
    ISSN: 1570-7458
    Keywords: JHA ; S-71639 ; hormonal control ; Colorado potato beetle ; metamorphosis ; diapause ; juvenile hormone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Résumé L'effet d'un analogue de l'hormone juvénile, S-71639, a été testé sur les oeufs, les quatre stades larvaires et les adultes du doryphore, Leptinotarsa decemlineata Say, par application topique ou après traitement de la plante-hôte. Le dernier stade larvaire est très sensible au S-71639. Le traitement de ce stade retarde le début de la métamorphose et empêche l'émergence adulte. Les animaux traités montrent de graves anomalies, mais ne sont pas immédiatement tués par les doses utilisées dans cette étude. Le traitement des larves perturbe aussi l'induction photopériodique de la diapause. Les adultes placés dans des conditions de diapause, commencent à pondre après traitement au S-71639. L'effet ovicide de la substance est plutôt faible. Les implications pour l'utilisation pratique du S-71639 dans la lutte contre le doryphore sont discutées.
    Notes: Abstract The effect of a juvenile hormone analogue, S-71639, was tested on the eggs, four larval instars and adults of the Colorado potato beetle, Leptinotarsa decemlineata Say, by topical application or after treatment of the foodplant. The last larval instar is very sensitive to S-71639. Treatment of this instar delayed the onset of pupation and prevented adult emergence. Treated animals showed severe abnormalities, but they were not immediately killed at the doses used in this study. Treatment of larvae also interfered with the photoperiodic induction of diapause. Adults, kept under diapausing conditions, started to lay eggs after treatment with S-71639. The ovicidal effect of the compound was rather weak. The implications for practical use of S-71639 in control of the Colorado potato beetle are being discussed.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Entomologia experimentalis et applicata 56 (1990), S. 1-13 
    ISSN: 1570-7458
    Keywords: Photoperiod ; diapause ; juvenile hormone ; JH titre ; corpus allatum ; neuropeptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 5 (1987), S. 255-269 
    ISSN: 0739-4462
    Keywords: lipoproteins ; Leptinotarsa decemlineata ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Lipophorin, the protein that specifically binds juvenile hormone in the hemolymph of the Colorado potato beetle, Leptinotarsa decemlineata, is a high-density lipoprotein of Mr ∼ 574,000. Lipophorin contains 43% lipid and is composed of two apoproteins: apolipophorin I (Mr ∼ 251,000) and apolipophorin II (Mr ∼ 78,000). Both apoproteins contain mannose residues. Carotenoids make up a substantial part of the lipid fraction. Lipophorin constitutes about 25% of the total hemolymph proteins. Its concentration in the hemolymph (26 μM in 4-day-old long-day and 40 μM in 4-day-old short-day beetles) changes with different physiological conditions concomitant with changes in total protein content. Lipophorin specifically binds 10R-juvenile hormone III with high affinity. The dissociation constant for 10R-juvenile hormone III is 12 ± 2 nM. One lipophorin molecule contains one specific juvenile hormone-binding site. The concentration of binding sites therefore equals that of lipophorin in hemolymph.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 7 (1988), S. 105-118 
    ISSN: 0739-4462
    Keywords: JH binding ; lipoprotein ; migratory locust ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The juvenile hormone binding protein in Locusta migratoria is a very high density lipoprotein of Mr ∼ 566,000. It contains 15% lipid and is composed of six seemingly identical subunits of Mr ∼ 77,000. It is a minor protein, constituting 1-2% of the total hemolymph proteins. Its concentration fluctuates with total protein content and follows a cyclic pattern related to the molting cycles.The binding protein has a high affinity for (10R)-juvenile hormone III. The dissociation constant for the hormone is 3.7 ∼ 0.6 nM, and one binding molecule contains six hormone-specific binding sites. The concentration of binding sites in the hemolymph is therefore very high, reaching a value of 26 μM in the last larval instar and 11 μM in the adult male.
    Additional Material: 7 Ill.
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