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Cytokinin oxidase fromZea mays kernels andVinca rosea crown-gall tissue

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Abstract

Cytokinin oxidase has been partially purified from matureZea mays kernels and fromVinca rosea corwn-gall tissue. The molecular weights of the two enzymes, determined by gel filtration, are very different: 94,400 (±10%) forZ. mays and 25,100 (±10%) forV. rosea. Specificity studies have been performed using a large number of synthetic and naturally occurring cytokinins. Only a small number of these compounds serve as substrates and both enzymes exhibit similar substrate specificity. In agreement with other workers, a Δ2 double bond in the N6 side chain is essential for activity. The presence of glucosyl or ribosyl groups in the 7-or 9-position or an alanyl group in the 9-position of the purine moiety have little effect on their susceptibility to cytokinin oxidase, but O-glucosyl derivatives are resistant to oxidation. The relevance of these enzyme systems to studies on cytokinin metabolism and to the endogenous cytokinins is discussed.

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Abbreviations

2iP:

N6–Δ2

2iPA:

N6–Δ2

HAP:

hydroxylapatite

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Authors and Affiliations

  1. Department of Botany and Microbiology, University College of Wales, SY23 3DA, Aberystwyth, Dyfed, UK

    Brian A. McGaw & Roger Horgan

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  1. Brian A. McGaw
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  2. Roger Horgan
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McGaw, B.A., Horgan, R. Cytokinin oxidase fromZea mays kernels andVinca rosea crown-gall tissue. Planta 159, 30–37 (1983). https://doi.org/10.1007/BF00998811

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  • DOI: https://doi.org/10.1007/BF00998811

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