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- Title
Purification and Characterization of Proteins from the 2S Fraction from Seeds of the Brassicaceae Family.
- Authors
MONSALVE, RAFAEL I.; RODRIGUEZ, ROSALIA
- Abstract
The 2S protein fractions from , , and 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 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 a I, the 2S protein from yellow mustard seeds. The obtained results suggest the existence of homology between the 2S albumins of Brassicaceae seeds.
- Publication
Journal of Experimental Botany, 1990, Vol 41, Issue 1, p89
- ISSN
0022-0957
- Publication type
Article