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  • 1990-1994  (6)
  • 1905-1909
  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (4)
  • Chilling  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Long-term chilling of young tomato plants under low light and subsequent recovery (1992)
    Springer
    Planta 186 (1992), S. 172-178 
    Details
    ISSN: 1432-2048
    Keywords: Chilling ; Growth (low temperature) ; Lycopersicon (chilling) ; Photosynthesis (chilling effects) ; Stomatal resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The influence of unfavourable climatic conditions at the onset of the growth period on chilling-sensitive tomato (Lycopersicon esculentum Mill., cv. Abunda) was studied by exposing young plants to combinations of low temperature and low light (60–100 μmol quanta · m−2 · s−1) for several weeks. When the temperature did not decrease below a critical point (8 ° C) no loss of developmental capacity of the plants was detected. However, while new leaves were readily formed upon return to normal growth conditions (22/18 °C, day/night, in a greenhouse), net accumulation of biomass showed a lag phase of approximately one week. This delay was accompanied by a strong, irreversible inhibition of photosynthesis in the fully expanded leaves which had been exposed to the chilling treatment. When plants were subjected to temperatures below 8 ° C, survival rates decreased after three weeks at 6 ° C and irreversible damage of apical meristematic tissue occurred. Drought-hardening prior to chilling ensured survival at 6 ° C and protected the plants against meristem loss.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00196246
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  • 2
    Electronic Resource
    Electronic Resource
    Long-term chilling of young tomato plants under low light and subsequent recovery (1992)
    Springer
    Planta 186 (1992), S. 179-187 
    Details
    ISSN: 1432-2048
    Keywords: Chilling ; Chlorophyll fluorescence ; Lycopersicon (chilling) ; Photoinhibition ; Photosynthate partitioning ; Photosynthesis (chilling effects) ; Ribulose-1,5-bisphosphate carboxylase/oxygenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To identify possible reasons for the persisting impairment of photosynthesis after long-term chilling, young tomato (Lycopersicon esculentum Mill.) plants were exposed to 6–10° C for two weeks under low illumination during the daily light period (60–100 μmol quanta · m−2 · s−1). The time courses of leaf carbohydrate contents, phosphorylated intermediates and chlorophyll-fluorescence parameters were followed. While starch formation was impaired during chilling at 6° C, soluble sugar contents increased from the first day onwards and reached up to eightfold the values found in unchilled plants within two weeks. At 8 and 10° C, a less drastic increase in soluble-carbohydrate contents was observed. During chilling, glucose-6-phosphate and fructose-6-phosphate accumulated up to 16 mM (assuming they are restricted to the cytoplasm). At the same time, non-photochemical quenching of chlorophyll fluorescence had increased and did not return to control values during the first week of recovery. The 3-phosphoglyceric acid/triose phosphate ratio remained nearly unaffected by the chilling treatment, indicating that the assimilatory power of the plants was still high even at the low temperatures. As a consequence of the chilling treatment, ribulose-1,5-biphosphate carboxylase/oxygenase (Rubisco) activity in the chilled leaves was irreversibly decreased. It is suggested that, in addition to a possible (orthophosphate-mediated) feedback inhibition by internal sugar accumulation, the low activity of Rubisco can play a significant role in the strong decrease of photosynthetic capacity during long-term chilling in tomato.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00196247
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  • 3
    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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  • 4
    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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  • 5
    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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  • 6
    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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