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  • 2000-2004  (2)
  • 2001  (2)
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  • 2000-2004  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    A variety of wheat tolerant to deep-seeding conditions: elongation of the first internode depends on the response to gibberellin and potassium (2001)
    Oxford, UK : Blackwell Science Ltd
    Plant, cell & environment 24 (2001), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The addition of gibberellin A3 (GA3) to culture media induced a dramatic elongation of the first internode in Hong Mang Mai, a wheat variety tolerant to deep-seeding conditions. The length of the first internode in the GA3-treated seedlings reached approximately 45 cm, which is twice as long as that of the control, whereas first internodes of other varieties were 3 to 12 cm long and hardly affected by GA3. The level of endogenous gibberellins (GA) in Hong Mang Mai was not greater than that of other wheat varieties. The expression of GAMyb, a transcription factor, was abundant in the first internode and substantially increased by GA3 application in Hong Mang Mai, compared with other wheat varieties. These results suggest that the first internode of Hong Mang Mai is more sensitive to GA in inducing strong elongation. The presence of potassium in the culture media was indispensable for the first internode elongation. Application of GA3 enhanced the uptake of potassium in Hong Mang Mai. Higher sensitivity of the first internode to GA could cause strong elongation by increasing the amount of osmotic solute, which plays an important role in the tolerance mechanism of Hong Mang Mai to deep-seeding conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3040.2001.00688.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Emulsifying and Surface Properties of Wheat Gluten under Acidic Conditions (2001)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The solubility of wheat gluten was greatly improved at pH 4 or lower where it showed good emulsifying activity. This might be due to its high surface activity in the acidic pH range and the formation of a stable protein film surrounding the oil droplets. Among the major gluten proteins, gliadins showed higher surface activity than glutenins. The content of glutenins in the adsorbed protein film was higher than that of gliadins, and glutenins are likely to have been adsorbed more tightly than gliadins. These results suggest that gluten proteins exhibit complex behavior, such as adsorption/desorption/displacement/rearrangement during the adsorption process in a gluten-stabilized emulsion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2001.tb16116.x
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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