
%0 Journal Article
%A Gillespie, JM 
%A Blagrove, RJ 
%T Isolation and Composition of the Seed Globulins of Winged Bean, <I>Psophocarpus tetragonolobus</I> (L.) DC
%J Functional Plant Biology
%D 1978/06/01
%V 5
%N 3
%P 357-369
%K 
%R https://doi.org/10.1071/PP9780357
%U https://www.publish.csiro.au/paper/PP9780357 
%X The amino acid composition of winged bean seed meal is similar to that of soybean but their storage globulins are quite different. Winged bean proteins are soluble to the extent of 60% at the pH of a meal-water slurry (pH 6.6), 80% at pH 11 but only 12% at pH 5. However, the proteins are soluble to the extent of 80% from pH 5 to 9 in 10% NaCl rising to 90% at pH 11. There are no satisfactory ways of recovering all the proteins from solution by simple changes in pH or ionic strength.    Winged bean seed contains major proteins with sedimentation coefficients of 2 S and 6 S. Electrophoresis on cellulose acetate resolves three globulin fractions which we have named psophocarpins A, B, and C. The proteins from these electrophoretic regions have been isolated and partially purified. Psophocarpin A is essentially a single protein comparatively rich in sulfur-containing amino acids while the other fractions are composed of a number of related components which have not been separated.    When examined by SDS-polyacrylamide gel electrophoresis, the globulin fractions differed in the kind of subunit proteins they contain and in the extent of disulfide bonding. The 40 000 mol. wt subunit of psophocarpin A contains disulfide bonded chains of mol. wt 16 000 and 24 000. The proteins corresponding to the other electrophoretic regions are more complex. 
