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  • Articles  (2)
  • 12-oxo-phytodienoic acid  (1)
  • Ceratophyllum (morphology  (1)
  • 1995-1999  (2)
  • 1965-1969
  • 1925-1929
  • Biology  (2)
  • Chemistry and Pharmacology
Collection
  • Articles  (2)
Publisher
Years
  • 1995-1999  (2)
  • 1965-1969
  • 1925-1929
Year
Topic
  • Biology  (2)
  • Chemistry and Pharmacology
  • 1
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana ; allene oxide synthase ; CYP74 ; octadecanoids ; jasmonate biosynthesis ; 12-oxo-phytodienoic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Allene oxide synthase, an enzyme of the octadecanoid pathway to jasmonates, was cloned from Arabidopsis thaliana as a full-length cDNA encoding a polypeptide of 517 amino acids with a calculated molecular mass of 58705 Da. From the sequence, an N-terminal transit peptide of 21 amino acids resembling chloroplast transit peptides was deduced. Three out of four invariant amino acid residues of cytochrome P450 heme-binding domains are conserved and properly positioned in the enzyme coding region, including the heme-accepting cysteine (Cys-470). Southern analysis indicated in A. thaliana only one allene oxide synthase gene to be present. While transcript levels were rapidly and transiently induced after wounding of the leaves, allene oxide synthase activity remained nearly constant at a low level of ca. 0.8 nkat per mg of protein. The cDNA encoding A. thaliana allene oxide synthase was highly expressed in bacteria giving rise to a polypeptide of the calculated molecular mass. The protein was enzymatically active, and verification of the reaction products by GC-MS showed that it was capable of utilizing not only 13-hydroperoxylinolenic acid (13-hydroperoxy-9(Z), 11(E), 15(Z)-octadecatrienoic acid), but also 13-hydroperoxylinoleic acid (13-hydroperoxy-9(Z), 11(E)-octadecadienoic acid) as substrate. The data suggest parallel pathways to jasmonates from linolenic acid or linoleic acid in A. thalina.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Key words: Biological life support ; Ceratophyllum (morphology ; physiology) ; Ecosystem (closed aquatic) ; Nitrate uptake
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The Closed Equilibrated Biological Aquatic System (CEBAS) consists of four subcomponents which form a closed (artificial) aquatic ecosystem initially designed to study the long-term influence of space conditions on several successive generations of aquatic organisms. Teleost fishes and water snails in the zoological component produce CO2, ammonium ions and waste compounds which can be utilized after ammonium is oxidised in a microbial component by the botanical component consisting of a rootless, aquatic higher plant species which eliminates ions, i.e. nitrate, and produces oxygen for animal respiration. An electronic component serves as a data-acquisition and regulation device for temperature and oxygen-dependent illumination of the plant chamber. A comprehensive interdisciplinary research programme, focused around the CEBAS, is especially well developed in the field of zoology. It covers a ground laboratory and preparations for two scheduled spaceflight projects, as well as aspects of combined animal-plant food production modules for human nutrition in bioregenerative space life-support systems and for terrestrial production sites. In the botanical research programme, morphological investigations on Ceratophyllum demersum L. performed with light and electron microscopy have demonstrated a gas lacuna system which, in addition to starch grains in the plastids, might regulate the buoyancy of the plant and/or serve as a `gas skeleton'. Also, a remarkable symmetry in the arrangement of tissues was observed in stems and older leaves. The photosynthetic capacities of Ceratophyllum in the CEBAS-MINI MODULE proved to be more than sufficient for life support, and experiments on nitrate uptake into the plants showed their capacity to utilize ions from the water.
    Type of Medium: Electronic Resource
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