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  • 1
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 55 (1986), S. 879-912 
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 14 (1991), S. 0 
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract. The levels of particular mRNAs in tomato leaves are altered in response to water stress. Certain transcripts appear as a consequence of the stress whereas others diminish in abundance. These changes were analysed by cell-free translation of leaf RNA followed by two-dimensional polyacrylamide gel electrophoresis of the translation products. Within 20 min of the onset of reduced leaf water potential in detached leaflets, stress-induced mRNAs appear in the transcript population. Other mRNAs accumulate more slowly and include among their in vitro translation products a prominently labelled group of polypeptides of about 18–19 kD. These transcripts are recovered from detached leaflets incubated for 2 and 8h at low water potential and from leaflets of intact plants that were stressed in situ for 10d. An additional water stress-induced mRNA that encodes a 64-kD polypeptide is detected in the transcript population from detached leaflets when [3H]glycine is used in place of [35S]methionine in the cell-free translations. Among the transcripts that decline in abundance as a consequence of water stress is an mRNA that encodes the small subunit of ribulose-1,5-bisphosphate carboxylase. Within 2h of rewatering stressed plants, certain mRNAs that were lost from the population return and those in the 18–19 kD range that are associated with the stress are not detectable.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Planta 162 (1984), S. 55-61 
    ISSN: 1432-2048
    Keywords: Hemagglutinin ; Lectin ; Triticum (wheat germ agglutinin)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Radioimmuno-and enzyme-linked immunosorbent assays show that a substantial amount of wheat germ agglutinin(WGA)-like protein is present at the base of the shoot and in the roots of adult wheat (Triticum aestivum L.) plants. The protein can be purified by hapten-and antibody-mediated affinity procedures. It forms an arc of identity with the embryo lectin upon Ouchterlony double-diffusion and is an active lectin that agglutinates trypsinized erythrocytes in an N-acetylglucosamine-and chitin-inhibitable manner. Reduced and carboxyamidated protein comigrates with the 18-kdalton subunits of embryo lectin on sodium dodecyl sulfate-polyacrylamide gels. Invivo labeling of 9-d-old, hydroponically grown plants with 35S-labeled sulfate demonstrates that at least some of the WGA-like protein is synthesized de novo. Immunocytochemistry with rabbit anti-WGA and colloidal-gold-conjugated second antibody shows that cross-reactive protein is present at the tips of new adventitious roots. In reactive cells, the lectin is localized near the inner surface of the vacuole membrane. Wheat plants contain up to 100 ng of WGA-like protein after the first week of growth, but the level fluctuates thereafter. Since most of the lectin is present at the base of the shoot and much less is found in older roots, these fluctuations may be the consequence of changes in the initiation of new advantitious roots.
    Type of Medium: Electronic Resource
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