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  • Electronic Resource  (4)
  • 1995-1999  (1)
  • 1985-1989  (3)
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  • Electronic Resource  (4)
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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 36 (1988), S. 69-73 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 94 (1995), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Maize (Zea mays L. cv. Pioneer 3925) endosperm development is sensitive to water deficit during rapid cell division and nuclear DNA endoreduplication. To gain insight into effects of water deficit on gene-products that are involved in these processes, we examined the accumulation of β-tubulin, a 50-kDa subunit of microtubules. Proteins extracted from endosperms were separated by SDS-PAGE and immunoblotted with antibodies to β-tubulin. In addition to the expected 50-kDa β-tubulin protein, monoclonal antibodies recognized a 35-kDa protein that predominated at early stages of development and progressively disappeared coincident with the appearance of 50-kDa β-tubulin. Various tests demonstrated that the cross-reacting 35-kDa protein was not a post-harvest artifact, but represented a group of in situ tubulin isotypes preferentially detected by the monoclonal antibodies we used. The pattern of appearance of the fragment suggested that differential expression or degradation of tubulin isotypes normally occurs during development. This expression pattern is prologed or altered during water deficit, which may affect cell division.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To gain understanding of the regulation of methionine level in plants, we assayed homoserine kinase and threonine synthase in extracts of wild type and several methionine-overproducing soybean [Glycine max (L.) Merr.] callus lines. The specific activity of homoserine kinase was depressed by 45–73%, and that of threonine synthase by 26–43% in the high methionine lines. Cysteine inhibited threonine synthase in wild type and variant lines. Threonine synthase in two variant lines showed significantly less inhibition by cysteine and in one line was inhibited by threonine. Depressed threonine synthase activity may increase the availability of homoserine phosphate to the competing methionine biosynthetic pathway.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Plant cell reports 7 (1988), S. 473-476 
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Several hundred soybean [Glycine max (L.) Merr.] cell lines resistant to ethionine were isolated either with or without chemical mutagenesis. of these, 26 were found to contain 2 to 22 times higher than normal levels of uncombined methionine. These 26 cell lines also contained higher than normal levels of S-adenosylmethionine and S-methylmethionine, but the levels of free lysine, threonine, cysteine, valine, tyrosine and phenylalanine were not elevated. Isoleucine levels were only slightly elevated. These results suggest that the regulation of methionine synthesis in vivo is more likely to be later in the pathway (after homoserine phosphate) than early in the pathway.
    Type of Medium: Electronic Resource
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