Modification of the oligomeric structure of 11 S globulin from sunflower (Helianthus annuus L.) and rape (Brassica napus L.) seeds by succinylation

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Abstract
The influence of various levels of succinylation on the structure of the 11S globulins from sunflower and rape seeds has been studied by the techniques of sedimentation velocity, viscometry and by circular dichroism spectroscopy in the near and far ultraviolet region. Both proteins dissociate gradually with increasing degree of succinylation forming 7S and 3–5S intermediates. At a level of 65–70% succinylation a 2S component occurs. The latter represents the final product of dissociation of the sunflower protein. The rapeseed protein dissociates further to smaller units. Contrary to the sunflower protein, the rapeseed protein shows an intermediate 11–14S associate at a level of 65–84% succinylation.The intrinsic viscosity of both proteins does not change remarkably until a succinylation of 65–70%, where a drastic viscosity increase is observed. At this level of modification a decrease of the positive circular dichroism bands in the near ultraviolet region takes place. Contrary to this, the negative ellipticity in the far ultraviolet region increases at a high level of modification, suggesting an enhancement of the amount of helix conformation.

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