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Isolation, properties, and structure of fraction I protein from Avena sativa L

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Summary

  1. 1.

    A method is described for the extraction and purification of Fraction I protein from Avena sativa L. leaves.

  2. 2.

    The protein possesses ribulose diphosphate carboxylase activity. Chromatography on gels of Sephadex G-200 separates phosphoribulokinase and ribose phosphate isomerase from the carboxylase.

  3. 3.

    The S°20w was calculated to be 18.2, the Stokes radius (determined by gel filtration on a cabibrated column) 74 Å, the molecular weight 5.7×105, and the frictional ratio 1.35.

  4. 4.

    An amino acid analysis is presented.

  5. 5.

    Electron microscope observations of negatively-stained Avena Fraction I protein molecules are compatible with the suggestion that they consist of 24 protomers disposed on the surface of an octahedral shell with 4:3:2 symmetry, and of diameter approximately 105 Å.

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Author notes

  1. M. W. Steer

    Present address: Department of Botany, University of Wisconsin, Madison, Wisconsin, USA

Authors and Affiliations

  1. Department of Botany, Queen's University of Belfast, Belfast 9, Northern Ireland

    M. W. Steer, B. E. S. Gunning, T. A. Graham & D. J. Carr

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  1. M. W. Steer
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  2. B. E. S. Gunning
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  3. T. A. Graham
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  4. D. J. Carr
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Steer, M.W., Gunning, B.E.S., Graham, T.A. et al. Isolation, properties, and structure of fraction I protein from Avena sativa L. Planta 79, 254–267 (1968). https://doi.org/10.1007/BF00396032

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  • DOI: https://doi.org/10.1007/BF00396032

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