Purification and characterization of napin-like proteins from radish

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Abstract
Nine 2S albumin proteins from garden and sea radish seeds (Raphanus sativus and Raphanus raphanistrum, respectively) have been purified. Their molecular weights and amino acid compositions have been determined. Most of these proteins exhibit a molecular mass of 14.5 kDa, but one component of each species shows a slightly higher value (15.1 kDa). The amino acid compositions obtained are typical of napin-like proteins, although a different content of Tyr and basic residues was observed. The isolated proteins present circular dichroism and fluorescence spectra nearly identical to each other, but different from those of rapeseed or mustard napins. The 2S albumins from radish exhibit about 53% α-helix, 14% β-bend, 16% β-turn and 17% aperiodic conformation. The microheterogeneity of these proteins has been analysed by high pressure liquid chromatography of the reduced molecules, and a high degree of polymorphism has been observed in most of the obtained fractions. On the basis of the amino acid contents of the individual chains, as well as the carboxypeptidase Y digestion data, new sites have been suggested for the processing of their polypeptide precursors to render the mature proteins.

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