Abstract
α and β globulin of azuki bean were fractionated from crude globulin fraction by salting out with 30% and 85% saturation of ammonium sulfate.
An examination of the composition of globulin components was performed by gel-filtration chromatography on a Sephadex G-200 column, determination of amino acid composition, N-terminal amino acid analysis and solubility test in aqueous sodium chloride solution.
β globulin was revealed to be main component of azuki bean protein and appeared homogeneous on gel filtration in 1 M sodium chloride solution. However, on solubility test it was shown heterogeneity and three N-terminal residues were detected.
