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Sulphydryl groups in the maintenance of the activity of binding protein for N-1-naphthylphthalamic acid fromAcer pseudoplatanus cells

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Biologia Plantarum

Abstract

Binding protein for N-1-naphthylphthalamic acid (NPA), an auxin transport inhibitor, was studied by analysis of the effects of reactions which modify particular amino acid side chains upon their binding activity. Na2SO3, N-ethylmaleimide (NEM) and dithiobisnitrobenzoic acid all inhibited the specific binding of NPA to its binding protein fromAcer pseudoplatanus L. cells. The presence of 10-6 M Na2SO3 in the binding assay reduced the affinity of the binding protein to NPA from Kd of 1.5 £ 10-8 M to Kd of 2.1 £ 10-8 M, while concentration of the binding protein was not significantly changed. When the same analysis was applied to NPA binding to the NEM-treated membrane particles, it was found that NEM inactivated binding without changing the affinity for NPA. This study revealed the importance of sulphydryl group(s) in the maintenance of NPA binding protein activity.

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Abbreviations

DTNB:

5’,5’-dithio-bis-2-nitrobenzoic acid

NEM:

N-ethylmaleimide

NPA:

N-1-naphthylphthalamic acid

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Author notes

  1. T. Xing

    Present address: Department of Botany, University of Toronto, 25 Willcocks Street, M5S 3B2, Toronto, Ontario, Canada

Authors and Affiliations

  1. The David Attenborough Laboratories, Department of Biological Sciences, De Montfort University, LE7 9SU, Leicester, England

    T. Xing, J. F. Hall, R. D. J. Barker & M. C. Elliott

Authors
  1. T. Xing
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  2. J. F. Hall
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  3. R. D. J. Barker
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  4. M. C. Elliott
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Xing, T., Hall, J.F., Barker, R.D.J. et al. Sulphydryl groups in the maintenance of the activity of binding protein for N-1-naphthylphthalamic acid fromAcer pseudoplatanus cells. Biol Plant 38, 47–51 (1996). https://doi.org/10.1007/BF02879632

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  • DOI: https://doi.org/10.1007/BF02879632

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