One- and two-dimensional gel electrophoresic identification of African yam bean seed proteins

J Agric Food Chem. 2000 Jun;48(6):2296-9. doi: 10.1021/jf990800x.

Abstract

Seed proteins were extracted from the African yam bean (AYB; Sphenostylis stenocarpa), an underutilized West African food legume. One- and two-dimensional polyacrylamide gel electrophoresis was then used to analyze the albumin fraction, galactose-specific lectins purified on immobilized galactose-Sepharose 4B, and abundant non-lectin seed proteins left over following affinity chromatography. N-terminal sequencing of prominently resolved polypetide bands led to identification of proteins having sequence homology with characterized legume seed proteins, namely, mung bean seed albumin, pea alpha-fucosidase, soybean Kunitz-type trypsin inhibitor, an endochitinase, pea pathogenesis-related protein, and/or cowpea seed storage proteins. Minor lectin-like proteins lacking hemagglutinating activity against rabbit and human erythrocytes were also identified. Because proteins such as protease inhibitors, chitinases, pathogenesis-related proteins, and lectins are known to have antimetabolic effects, the findings from this study may have relevance in the acceptability, adoption, and utilization of AYB as human food.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Electrophoresis, Gel, Two-Dimensional / methods
  • Electrophoresis, Polyacrylamide Gel / methods
  • Fabaceae / chemistry*
  • Hemagglutination Tests
  • Humans
  • Lectins / analysis
  • Lectins / chemistry
  • Lectins / pharmacology
  • Molecular Sequence Data
  • Nutritive Value
  • Peptide Fragments / chemistry
  • Plant Lectins
  • Plant Proteins / analysis*
  • Plant Proteins / chemistry
  • Plants, Medicinal*
  • Rabbits
  • Seeds / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Lectins
  • Peptide Fragments
  • Plant Lectins
  • Plant Proteins