2S albumin from buckwheat (Fagopyrum esculentum moench) seeds.
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.
Radovic
R S
RS
Faculty of Biology, University of Belgrade, Yugoslavia.
Maksimovic
R V
RV
Brkljacic
M J
MJ
Varkonji Gasic
I E
IE
Savic
P A
PA
D055516:2S Albumins, Plant; D000596:Amino Acids / Q000032:analysis; D052179:Antigens, Plant; D002499:Centrifugation, Density Gradient; D004591:Electrophoresis, Polyacrylamide Gel; D019612:Fagopyrum / Q000737:chemistry*; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011498:Protein Precursors / Q000737:chemistry* / Q000302:isolation & purification; D012639:Seeds / Q000737:chemistry*
D055516:2S Albumins, Plant; D000596:Amino Acids; D052179:Antigens, Plant; D010940:Plant Proteins; D011498:Protein Precursors