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Purification and properties of three albumins from Triticum aestivum seeds
Author(s) -
Cantagalli P.,
Di Giorgio G.,
Morisi G.,
Pocchiari F.,
Silano V.
Publication year - 1971
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740220510
Subject(s) - bromophenol blue , sephadex , isoelectric point , size exclusion chromatography , chromatography , polyacrylamide gel electrophoresis , electrophoresis , chemistry , polyacrylamide , glycine , albumin , yield (engineering) , isoelectric focusing , amino acid , biochemistry , enzyme , materials science , polymer chemistry , metallurgy
Three albumins were isolated from bread wheat seeds by gel filtration on Sephadex G‐100 and differential preparative disc‐electrophoresis on polyacrylamide gel. The proteins were obtained in sufficient yield and purity to carry out characterisation studies. The electrophoretic mobilities of the three albumins in polyacrylamide discs in glycine—Tris medium, pH 9·5, were 0·28, 0·34 and 0·39 (referred to that of bromophenol blue taken as 1). The isoelectric points were 6·40, 6·40 and 5·35 and the molecular weights 17, 700, 18, 200 and 18, 900, respectively. The amino acid compositions of the purified albumins were very similar. The correlation of the purified albumins with those isolated from bread wheats by other authors is discussed.