| Abstract: | Winged bean proteins were extracted by a pH 9.5, 0.3M borate extraction medium. The extracted proteins were fractionated by Sepharose CL-6B gel filtration chromatography into four fractions. Fraction 2 (F2, mol. wt 200 000) and Fraction 3 (F3, mol. wt 35 000) are the two major protein fractions. F3 was further resolved into Fraction 3A (F3A, mol. wt 44 160) and Fraction 3B (F3B, mol. wt 23 700) by Sephadex G-75 gel filtration chromatography. Both F2 and F3 fractions were heterogeneous when examined by polyacrylamide gel electrophoresis method. There are some varietal variations in the distribution of winged bean protein fractions recovered by gel filtration chromatography. Trypsin inhibitor and chymotrypsin inhibitor activity were found only in F3B, whereas haemagglutinating activity was found only in F3A. |
