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- W1988544057 abstract "An improved procedure for the isolation and purification of the 11 S globulin from sunflower seeds (helianthinin) is described, including a combined purification by gel chromatography and ionexchange chromatography. The protein has a sedimentation constant of s20, w = 12.8 x 10−13 s, a Stokes radius of 57 Å and a diffusion constant of 3.76 x 10−7 cm2 s−1 (the last two derived from gel chromatographic analysis). Hence it follows a molecular weight of Ms, D = 305000. The isoelectric point determined by isoelectric focusing lies at pH 4.7. High contents of glutamic (26%) and aspartic (14%) acid and arginine (9.7%) as well as a low content of sulphur containing amino acids are characteristic for the amino acid composition. 59% of the acidic amino acids are present in an amidated form. The globulin contains 12 disulphide bridges per molecule." @default.
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- W1988544057 date "1979-01-01" @default.
- W1988544057 modified "2023-10-14" @default.
- W1988544057 title "On seed proteins Part 11. Purification, Chemical Composition, and Some Physico-chemical Properties of the 11 S Globulin (Helianthinin) in Sunflower Seed" @default.
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- W1988544057 doi "https://doi.org/10.1002/food.19790230309" @default.
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