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  • Abscisic acid  (2)
  • Springer  (2)
  • American Geophysical Union (AGU)
  • American Physical Society (APS)
  • Nature Publishing Group
  • 1975-1979  (2)
  • 1945-1949
Collection
Publisher
  • Springer  (2)
  • American Geophysical Union (AGU)
  • American Physical Society (APS)
  • Nature Publishing Group
Years
  • 1975-1979  (2)
  • 1945-1949
Year
  • 1
    ISSN: 1432-2048
    Keywords: Abscisic acid ; Amylase ; Cereal kernel ; Germination (seeds) ; Gibberellin ; Triticale
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Abscisic-acid (ABA) levels were determined in triticale 6A190 kernels at various stages of development from anthesis to maturity. ABA reached a maximum at ca. 22 d post-anthesis and declined rapidly 12 d later. Associated with drying of the kernel at maturity there was a rapid increase in the endogenous level of α-amylase, apparently based upon de-novo synthesis. Simultaneously there were visible signs of degradation of the large starch grains in the starchy endosperm. Regulation of α-amylase production in the kernel by exogenous gibberellic acid (GA3) was only evident in the almost mature kernel (30–40 d after anthesis) and then only if these kernels were first dried artificially. Furthermore, little α-amylase mRNA could be detected prior to kernel maturity and water loss. Thus, the high levels of gibberellin (GA) that have been found early in kernel development in cereals do not appear to control the later production of α-amylase and onset of kernel germination in the ear of triticale. However, the presence of high levels of ABA until maturity could prevent early germination and premature production of α-amylase. Kernels of triticale 6A190 are characteristically shrivelled and non-dormant at maturity. The relevance of changes in the capacity of kernels to respond to and produce GA and ABA is discussed in relation to problems of harvest dormancy in cereals.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Planta 138 (1978), S. 303-304 
    ISSN: 1432-2048
    Keywords: Abscisic acid ; Binding assay ; Hormone binding ; Plasma membranes ; Vicia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A centrifugation binding assay has been used to demonstrate the binding of [3H] (±) abscisic acid to membrane-rich fractions prepared from leaves of Vicia faba L. Kinetic analysis of this binding shows evidence of saturation of binding sites with increasing concentration of ligand. Scatchard analysis of these data yields a biphasic plot possibly indicating the presence of two types of binding sites. The dissocation constant for the high affinity site has been calculated to be 3.5×10-8 mol 1-1.
    Type of Medium: Electronic Resource
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