Electrophoretic separation and properties of winged bean seed trypsin inhibitor

1981 ◽  
Vol 32 (5) ◽  
pp. 443-450 ◽  
Author(s):  
David F. Hildebrand ◽  
Navagnana S. Hettiarachchy ◽  
Theodore Hymowitz ◽  
John W. Erdman
Keyword(s):  
Trypsin Inhibitor ◽  
Winged Bean ◽  
Electrophoretic Separation ◽  
Bean Seed

Blood-pressure lowering efficacy of winged bean seed hydrolysate in spontaneously hypertensive rats, peptide characterization and a toxicity study in Sprague-Dawley rats

2018 ◽  
Vol 9 (3) ◽  
pp. 1657-1671 ◽  
Author(s):  
Shyan Yea Chay ◽  
Annas Salleh ◽  
Nor Fazila Sulaiman ◽  
Najib Zainal Abidin ◽  
Mohamad Ariff Hanafi ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Spontaneously Hypertensive Rats ◽  
Good Manufacturing Practice ◽  
Reduce Blood Pressure ◽  
Winged Bean ◽  
Bean Seed ◽  
Sprague Dawley ◽  
Hypertensive Rats ◽  
Spontaneously Hypertensive ◽  
Pressure Lowering

Winged bean seed hydrolysate is found to reduce blood pressure in spontaneously hypertensive rats. Peptide of non-Current Good Manufacturing Practice grade demonstrates toxicity and is not suitable for testing in animals.

Isolation and Composition of the Seed Globulins of Winged Bean, Psophocarpus tetragonolobus (L.) DC

1978 ◽  
Vol 5 (3) ◽  
pp. 357 ◽  
Author(s):  
JM Gillespie ◽  
RJ Blagrove
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Winged Bean ◽  
The Other ◽  
Bean Seed ◽  
Psophocarpus Tetragonolobus ◽  
Disulfide Bonding ◽  
Single Protein ◽  
Seed Globulins ◽  
Sulfur Containing

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.

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