The problem of refolding and reassembling recombinant vicilin subunits
1990
Chambers, S.J. | Carr, H.J. | Plumb, G.W. | Lambert, N.
The reassociation of a storage protein (pea (Pisum sativum L) vicilin) expressed in yeast (Saccharomyces cerevisiae MC16 (ade 2-1, leu 2-3, lys 2-1, his 4-712FS, SUF 2)) was investigated. The corresponding protein in bean (Phaseolus vulgaris L), termed phaseolin, was used as a mode, to produce a methodology for the refolding of the recombinant protein. Phaseolin was successfully renatured from its dissociated state in 5 M guanidinium chloride. Application of this rationale to yeast-derived vicilin proved unsuccessful. The nature of the yeast vicilin and its failure to refold and reassemble correctly are discussed together with the further experimental approaches required.
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