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  • 1
    Electronic Resource
    Electronic Resource
    Preface (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 1-2 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030702
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  • 2
    Electronic Resource
    Electronic Resource
    Premature production of late larval storage proteins in larvae of trichoplusia ni parasitized by euplectrus comstockii (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 97-109 
    Details
    ISSN: 0739-4462
    Keywords: Hymenoptera ; venom ; host hemolymph ; plasma proteins ; regulation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Investigations were conducted to determine the titer of storage proteins in larvae of the cabbage looper, Trichoplusia ni (Hübner), that were parasitized by the ectoparasitoid Euplectrus comstockii Howard (Hymenoptera: Eulophidae). A gradual increase was noted in the titer of the storage proteins present in the hemolymph of parasitized third and fourth instar larvae and in the hemolymph of isolated thoracic and abdominal tissues of fourth instar larvae. The final amount present in parasitized third and fourth instar larvae was similar to that found in nonparasitized fifth instar larvae. The stimulation of storage proteins in envenomed larvae demonstrates the ability (competence) of early larval stages to produce a gene product that normally occurs in the last larval stadium of the lepidopteran larval host. The gene expression necessary for storage protein production in isolated tissues may be altered by mechanisms separate from inherent developmental processes and the intact endocrine system. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940260204
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  • 3
    Electronic Resource
    Electronic Resource
    In vitro translation of diapause mRNA from the fat body of active and diapause larvae of the pink bollworm, Pectinophora gossypiella (Saunders) (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 23 (1993), S. 1-11 
    Details
    ISSN: 0739-4462
    Keywords: diapause protein ; poly(A)+ RNA ; larval diapause ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A diapause associated protein (DAP) (Mr 103,000) was isolated from the hemolymph and fat body of diapausing fourth instar larvae of the pink bollworm Pectinophora gossypiella. The protein has been named Pectinophora diapause protein (PDP). The in vitro translation peptide patterns of total RNA from the fat body of actively feeding fourth instar, wandering, prediapause, early diapause, mid-diapause, and late diapause larvae in rabbit reticulocyte lysates showed the presence of poly (A)+ RNA sequence of PDP. The antigen was immuno-precipitated by polyclonal antiserum. It was concluded that the transcription of the PDP gene in the fat body cells started in the late fourth instar larva and that the expression of this gene was regulated at the level of transcription in the fat body of diapausing larvae. Northern hybridization analysis revealed that wandering fourth instar larvae (diapause individuals) maintain a relatively low level of diapause message (mRNA/2.4 kb) in their fat body cells which may be necessary for the induction of diapause. © 1993 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940230103
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  • 4
    Electronic Resource
    Electronic Resource
    Sex pheromone blend of Manduca sexta: Responses of central olfactory interneurons to antennal stimulation in male moths (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 10 (1989), S. 281-291 
    Details
    ISSN: 0739-4462
    Keywords: antennal lobe ; electrophysiology ; olfaction ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Recently, chemical analysis of solvent rinses of the external surfaces of pheromone glands from female Manduca sexta revealed a blend of 12 aldehydes, including the previously identified sex pheromone component, (E,Z)-10,12-hexadecadienal (bombykal). Previous electrophysiological studies showed that olfactory (deutocerebral) interneurons in the antennal lobes of males exhibited a wide range of responsiveness to pheromonal stimulation of the ipsilateral antenna. These experiments were performed with crude extracts of pheromone glands as well as two synthetic compounds: the major pheromone component, bombykal, and (E,Z)-11,13-pentadecadienal, a mimic of a second component of the female's pheromone blend. Using intracellular methods, we have now reexamined similar olfactory interneurons, using each of the 12 chemically identified components as well as synthetic blends of various combinations of them. Eight of the 12 components isolated from female glands elicited some form of response in olfactory interneurons in males. In accordance with biochemical and behavioral data, the most potent are bombykal and two trienals, (E,E,E)- and (E,E,Z)-10,12,14-hexadecatrienal. We also conclude that the C15 dienal is selective for one of the trienal receptors on the antenna, but is much less potent than the natural trienal stimulant.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940100404
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  • 5
    Electronic Resource
    Electronic Resource
    Developmental responses of Trichoplusia ni (Lepidoptera: Noctuidae) to parasitism by the ectoparasite Euplectrus plathypenae (Hymenoptera: Eulophidae) (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 13 (1990), S. 83-94 
    Details
    ISSN: 0739-4462
    Keywords: molt arrest ; 20-hydroxyecdysone ; juvenile hormone ; methoprene ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Parasitism by Euplectrus plathypenae inhibits larval-larval ecdysis in Trichoplusia ni by injecting nonparalytic factor(s) into the host during the stinging process via the parasitoid's ovipositor. The parasitized host moves freely, feeds, and gains weight prior to the time of the normal ecdysis but does not molt. Parasitoid development is not required for the expression of molt arrest in the host. Parasitism during the first three fourths of the larval stadium results in molt arrest. Arrestment of molting is independent of 20-hydroxyecdysone and juvenile hormone. The arrestment factor(s) affect the epidermal tissue of the thorax and abdomen in ligated hosts without apparent interaction from other areas of the body. Cuticle and epidermal tissue of parasitized insects do not show signs of apolysis or ecdysis.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940130108
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  • 6
    Electronic Resource
    Electronic Resource
    A diapause associated protein of the pink bollworm Pectinophora gossypiella saunders (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 21 (1992), S. 1-11 
    Details
    ISSN: 0739-4462
    Keywords: hemolymph proteins ; diapause protein ; larval diapause ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A diapause associated protein was electrophoretically isolated from the hemolymph of diapausing last instar larvae of the pink bollworm Pectinophora gossypiella. This protein (Mr ∼490,000, glycolipoprotein) was given the name Pectinophora diapause protein (PDP). It is composed of one subunit (Mr 103,000). The concentration of PDP increased dramatically in the hemolymph of diapausing larvae from 17.4% in prediapause (PD) phase to 29.2% in early diapause (ED) phase reaching a level of 38.6% in larval hemolymph of middiapause (MD) phase. The concentrations of total proteins in the hemolymph of active feeding (A), PD, ED, and MD larvae were 69.8, 106.6, 113.3, and 118 mg/ml, respectively, while those in the fat body of the same larvae were 7.1, 7.4, 8.8, and 4.5 mg/g, respectively. In Pectinophora a drop in the concentration of fat body proteins coincided with a corresponding increase in hemolymph proteins, which suggests an active release of protein from the fat body into the hemolymph during the development of diapause. A partial amino acid sequence of pectinophorin showed the first 15 amino acids starting from the amino terminus of the peptide chain: N-ALA-LYS-THR-ILEU-VAL-GLU-ASN-MET-PRO-PRO-THR-PRO-LEU-ASN-ALA-C. © 1992 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940210102
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