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Purification and Characterization of Proteins from the 2S Fraction from Seeds of the Brassicaceae Family

RAFAEL I. MONSALVE and ROSALIA RODRIGUEZ
Journal of Experimental Botany
Vol. 41, No. 222 (January 1990), pp. 89-94
Published by: Oxford University Press
Stable URL: http://www.jstor.org/stable/23692405
Page Count: 6
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Purification and Characterization of Proteins from the 2S Fraction from Seeds of the Brassicaceae Family
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Abstract

The 2S protein fractions from Brassica rapa, Brassica oleracea, and Brassica napus seeds have been obtained and their components purified and characterized. These albumins represent about 13% of the total seed protein extracted with saline buffer. The calculated molecular weights of the eleven purified proteins are very similar, about 14 500 Daltons, although two components isolated from B. napus exhibit a lower molecular weight. The amino acid compositions of the isolated proteins present a series of common features: a high content of Cys and basic residues as well as a very high amount of Pro (15%) and Glx (30%). The eleven purified proteins cross-react with antibodies against Sin a I, the 2S protein from yellow mustard seeds. The obtained results suggest the existence of homology between the 2S albumins of Brassicaceae seeds.

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