Add time:08/11/2019         Source:sciencedirect.com

The small Mr, proteins of sunflower seed (Helianthus annuus) are soluble in 60% (by vol) methanol. These proteins, classified as albumins on the basis of their solubility in water, were isolated from a salt extract of sunflower seed by precipitating the 11S globulins with 60% (by vol) methanol and were resolved into eight distinct components by reversed-phase HPLC. Electrophoresis showed that each fraction contained a single polypeptide chain with an apparent Mr, in the range 10 000–18 000. The individual sunflower albumins are basic proteins with distinct amino acid compositions. The major albumins (4–8) contain high contents of glutamine/glutamic acid, asparagine/aspartic acid, arginine and cysteine, characteristic of the 2S class of seed storage proteins. One exception was the small glutamine/glutamic acid content of albumin 6. Two of the sunflower albumins (7 and 8) with Mr - 10 000 were methionine-rich proteins containing 16 residues per cent methionine as well as eight residues per cent cysteine. These sulphur-rich proteins constitute some 7% of the total salt extractable seed protein. A method for the preparation of these two albumins using a reversed-phase Sep-pak cartridge is described.

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