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  • ACC oxidase  (1)
  • Analytical Chemistry and Spectroscopy  (1)
  • 1
    ISSN: 1573-5028
    Keywords: ACC oxidase ; differential/gene expression ; Helianthus annuus ; silver ions ; wounding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In an effort towards understanding the biochemical properties and physiological functions of 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase homologues, we have isolated three ACC oxidase clones from sunflower (Helianthus annuus) seedlings. ACCO1 is a cDNA clone while ACCO2 and ACCO3 and reverse transcriptase-polymerase chain reaction clones. Southern analysis indicated the existence of at least three members in the sunflower ACC oxidase gene family. Expression studies showed that ACCO3 was equally expressed in leaves, hypocotyl, and roots of sunflower seedlings, but it constituted only a small amount of the total ACC oxidase transcripts. In contrast, ACCO1 and ACCO2 were differentially expressed in these organs. ACCO1 mRNA was most abundant in roots, whereas ACCO2 was the major homologue in leaves and in hypocotyl. The levels of total ACC oxidase transcripts in these organs were also determined. High ACC oxidase transcript levels were associated with tissues containing rapidly dividing cells. Wounding and silver ion treatments of hypocotyls increased ACC oxidase mRNA levels and ACC oxidase activity; these events being consistent with the increases in ethylene production. In contrast, ACC oxidase protein levels were not affected by these treatments, suggesting that either a translational regulation and/or a rapid turn-over of the protein is involved in both wound- and silver ion-induced gene expression. Contrary to data in the literature, we found that auxins, ethephon and ACC did not affect ACC oxidase mRNA levels in sunflower hypocotyls. The complexity of ACC oxidase regulation and the significance of organ differential expression of ACC oxidase genes are discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 31 (1993), S. S110 
    ISSN: 0749-1581
    Keywords: NMR ; 113Cd NMR ; Transferrin ; Hydrogencarbonate ; N-lobe ; C-lobe ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The binding of Cd2+ to human serum transferrin (80 kDa) was studied by 113Cd NMR spectroscopy. At pH 7 in the presence of hydrogen-carbonate as synergistic anion, two resonances of similar intensity at 38.1 and 43.6 ppm were observed, consistent with Cd2+ binding to oxygen ligands and one nitrogen ligand in the specific metal-binding clefts of the N- and C-lobes of the protein.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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