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  • Binding site (ethylene)  (2)
  • Hormone binding  (2)
  • EBP  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Studies on ethylene binding by cell-free preparations from cotyledons of Phaseolus vulgaris L. (1980)
    Springer
    Planta 148 (1980), S. 397-406 
    Details
    ISSN: 1432-2048
    Keywords: Ethylene binding ; Hormone binding ; Phaseolus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The preparation is described of a cell-free system from developing cotyledons of Phaseolus vulgaris cv. Canadian Wonder which is capable of binding ethylene. The binding is saturable and the apparent dissociation constant for ethylene is 6.4·10-10 M in solution. The binding site is associated with subcellular particles and treatment with Triton X-100 results in substantial solubilisation of the activity. The kinetics of association and dissociation of the ligand and the binding site are described. The system is heat labile and binding activity is diminished by treatment with some proteolytic enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388129
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Studies on ethylene binding by cell free preparations from cotyledons of Phaseolus vulgaris L. (1980)
    Springer
    Planta 148 (1980), S. 407-411 
    Details
    ISSN: 1432-2048
    Keywords: Ethylene binding ; Hormone binding ; Phaseolus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Various protein reactive agents such as dithioerythritol, dithiothreitol, mercaptoethanol and p-chloromercuribenzoate inhibit binding of ethylene to cell free preparations of Phaseolus vulgaris L. The effect of the thiols is partially reversed by treatment with diamide; occupation of the binding site by ligand diminishes the inhibition caused by p-chloromercuribenzoate but not that caused by thiols. Growth regulators other than ethylene do not affect binding. Physiologically active structural analogues of ethylene competitively inhibit binding of the growth regulator and their relative effectiveness in the cell free system closely resembles that in developmental processes controlled ethylene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388130
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    Paper (German National Licenses)
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  • 3
    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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    Paper (German National Licenses)
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  • 4
    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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    Paper (German National Licenses)
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  • 5
    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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