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Seed Proteins pp 241–257Cite as

Canavalin

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Abstract

In the early years of the twentieth century the noted biochemist J. D. Sumner began his quest to purify an enzyme and to show that it was a homogeneous protein entity and not simply a colloidal dispersion. He intended to prove his assertion, which was at that time fiercely contested, by demonstrating that the purified enzyme could be crystallized, the classical proof of chemists everywhere that a pure and singular compound had been obtained. Proof of his thesis was eventually achieved by Sumner in exactly this way (Sumner, 1926), for which he shared the Nobel Prize with Northrup and Stanley in 1936. Sumner’s second, equally important contribution to biochemistry was his development of methods for the crystallization of proteins. Indeed, the globulins of the Jack Bean played a salient role in Sumner’s success and canavalin, in particular, has continued to play a major role in the development of modern crystallization technologies for X-ray diffraction analysis and protein engineering.

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Authors and Affiliations

  1. Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, 92697-3900, USA

    Alexander Mcpherson

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  1. Alexander Mcpherson
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Peter R. Shewry Rod Casey

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© 1999 Springer Science+Business Media Dordrecht

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Mcpherson, A. (1999). Canavalin. In: Shewry, P.R., Casey, R. (eds) Seed Proteins. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4431-5_11

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  • DOI: https://doi.org/10.1007/978-94-011-4431-5_11

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-5904-6

  • Online ISBN: 978-94-011-4431-5

  • eBook Packages: Springer Book Archive

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