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  • 1
    Electronic Resource
    Electronic Resource
    Partial purification of an ethylene-binding site from Phaseolus vulgaris L. cotyledons (1985)
    Springer
    Planta 164 (1985), S. 272-277 
    Details
    ISSN: 1432-2048
    Keywords: Binding site (ethylene) ; Ethylene (binding site) ; Phaseolus (ethylene binding)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The solubilised ethylene-binding site (EBS) of Phaseolus vulgaris L. cotyledons is an asymmetrical protein with a sedimentation coefficient of 2 S and a Stoke's radius of 6.1 nm (determined by ultracentrifugation on isokinetic gradients and gel-permeation chromatography, respectively). The molecular weight and frictional ratio were calculated as 52 000–60 000 and 2.37–2.48, respectively. The EBS has an isoelectric point at between pH 3–5, determined by isoelectric focussing and exhibits a negative charge at pH 8 during non-denaturing electrophoresis. The electrical charge on the EBS is shielded; the EBS does not bind to anion-exchange media under the experimental conditions reported here, is not precipitated by ammonium sulphate and does not precipitate at its isoelectric pH. The EBS preferentially partitions into detergent phases. The results indicate that the EBS is a hydrophobic protein complexed with detergent in aqueous solution. The techniques used to characterise the EBS also resulted in varying degress of purification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00396092
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  • 2
    Electronic Resource
    Electronic Resource
    The effect of solubilisation on the character of an ethylene-binding site from Phaseolus vulgaris L. cotyledons (1984)
    Springer
    Planta 160 (1984), S. 474-479 
    Details
    ISSN: 1432-2048
    Keywords: Binding site (ethylene) ; Ethylene (binding site) ; Phaseolus (ethylene binding)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ethylene-binding site (EBS) from Phaseolus vulgaris cv. Canadian Wonder cotyledons can be solubilised from 96,000 g pelleted material by Triton X-100 or sodium cholate. Extraction of 96,000 g pellets with acetone, butanol or butanol and ether results in a total loss of ethylene-binding activity. Like the membrane-bound form, the solubilised EBS has an apparent KD(liquid) of 10-10 M at a concentration of 32 pmol EBS per gram tissue fresh weight. Propylene and acetylene act as competitive inhibitors, carbon dioxide appears to promote ethylene binding and ethane has no significant effect. The solubilised EBS is completely denatured affect. The solubilised EBS is completely denatured after 10 min at 70°C, by 1 mM mercaptoethanol and 0.1 mM dithiothreitol, but not by trypsin or chymotrypsin. However, solubilisation decreases the rate constant of association from 103 M-1 s-1 to 101–102 M-1 s-1 and hence does not permit experimental determination of the rate constant of dissociation. The pH optimum for ethylene binding is altered from the range pH 7–10 in the membrane-bound form to the pH range 4–7 in the solubilised form. The EBS appears to be a hydrophobic, intergral membrane protein, which requires a hydrophobic environment to retain its activity. Partitioning of the EBS into polymer phases is determined by the detergent used for solubilisation indicating that when solubilised, the EBS forms a complex with detergent molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00429766
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  • 3
    Electronic Resource
    Electronic Resource
    Ethylene binding sites in higher plants (1996)
    Springer
    Plant growth regulation 18 (1996), S. 71-77 
    Details
    ISSN: 1573-5087
    Keywords: Arabidopsis ; ethylene ; ethylene binding protein ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract A review of work carried out on ethylene binding in higher plants is presented. The use of radio-labelled displacement assays has identified specific 14C-ethylene binding in all tissues so far studied. virtually all higher plants studied contain at least two classes of ethylene binding site, one of which fully associates and dissociates in about 2 h and a class of sites that takes up to 20 h to become fully saturated. Although the types of site differ in their rate constants of association they have similar and high affinities for ethylene. A series of Arabidopsis thaliana mutants shown to vary in sensitivity to ethylene have been analysed for 14C-ethylene binding. One mutant, eti 5, which was shown to be unaffected by ethylene concentrations of up to 10,000 μL L−1 was also shown to exhibit reduced binding. In vivo and in vitro studies on pea have shown that ethylene binding can be detected in this tissue. In vitro studies have shown that both membrane and cytosolic fractions contain measurable amounts of ethylene binding. Interestingly, cytosolic ethylene binding consisted only of the fast associating/dissociating type. Developing cotyledons of Phaseolus vulgaris contain a higher concentration of ethylene binding sites that other tissues and only contain the slow dissociating component. These facets have allowed the purification of ethylene binding protein(s) (EBP) from this tissue. The proteins which bind ethylene can be resolved into two bands of 26 and 28 kDa on semi-denaturing PAGE and the proteins appear to be single entities on a 2-D gels. Data will be presented which indicate a possible role for heterotrimetric G-proteins in the early stages of the ethylene signal transduction pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028490
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  • 4
    Electronic Resource
    Electronic Resource
    Studies on the possible role of protein phosphorylation in the transduction of the ethylene signal (1996)
    Springer
    Plant growth regulation 18 (1996), S. 135-141 
    Details
    ISSN: 1573-5087
    Keywords: Arabidopsis ; EBP ; ethylene ; phosphorylation ; receptors ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Previous work in our laboratory has demonstrated the existence of high affinity binding sites for the plant growth regulator ethylene. The ethylene binding protein (EBP), from Phaseolus cotyledons, shows many of the characteristics of a functional receptor for ethylene, has been purified on SDS-PAGE and polyclonal antibodies raised in rabbits. Current work involves the investigation of the ethylene transduction signal in a number of ethylene-responsive tissues. In peas, it has been shown that ethylene promotes the phosphorylation of specific proteins of similar molecular weight to the EBP from Phaseolus. Such ethylene-induced phosphorylation can be inhibited by the ethylene antagonist, 2,5-NBD. The antibodies raised to the EBP from Phaseolus have been shown to immunoprecipitate 32P-labelled proteins from membrane protein preparations obtained from pea tissue. Studies on ethylene binding in pea have also shown that the binding of ethylene may be regulated by phosphorylation. Thus, under conditions which promote phosphorylation, binding is inhibited, whereas the reverse is true under conditions which enhance dephosphorylation. Further work is described which examines the effect of protein kinase, protein phosphatase and calcium channel inhibitors on ethylene-induced phosphorylation in peas, together with wild-type (WT) and ethylene insensitive (eti) mutants of Arabidopsis thaliana. The effects of these treatments can be monitored in vivo using the ethylene-induced triple response as a screen. Furthermore, the protein profiles of such treated seedlings can then be compared by labelling protein extracts with 32P and subjecting the samples to SDS-PAGE followed by autoradiography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028498
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    Paper (German National Licenses)
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