2S albumin from buckwheat (Fagopyrum esculentum Moench) seeds
1999
Radovic, R.S. | Maksimovic, R.V. | Brkljacic, M.J. | Varkonji Gasic, I.E. | Savic, P.A.
Sucrose density gradient centrifugation showed that approximately 30% of total buckwheat proteins migrated with a 2S sedimentation coefficient. The main part of that fraction, polypeptides in the range of molecular mass from 8 to 16 kDa, were water soluble and represented albumins. SDS-PAGE analysis in nonreducing and reducing conditions showed that these polypeptides were not linked by disulfide bonds. The albumins make 25% of total salt soluble proteins, but that content is dramatically reduced under S-deficiency conditions. Determination of amino acid composition showed high methionine (9.2%) and lysine (5.6%) contents. That characteristic offers the possibility of transfer of the genes for individual albumin polypeptides to legumes and cereals limited in those essential amino acids to improve their nutritional quality.
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