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Purification and properties of three albumins from Triticum aestivum seeds

✍ Scribed by P. Cantagalli; G. Di Giorgio; G. Morisi; F. Pocchiari; V. Silano

Publisher: John Wiley and Sons
Year: 1971
Tongue: English
Weight: 398 KB
Volume: 22
Category: Article
ISSN: 0022-5142
DOI: 10.1002/jsfa.2740220510

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✦ Synopsis

Abstract

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.

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