Purification and characterization of high salt-soluble vicilin from mung bean (Vigna radiata).
We report a method for the purification of vicilin from mung bean (Vigna radiata) mainly on the basis of solubility of mung bean vicilin even in high salt. Mung bean vicilin remains in solution even after 90% relative saturation of ammonium sulphate. The resulting supernatant after dialysis was subjected to gel filtration (Sephadex G-150) to remove other contaminant polypeptides, and finally the protein was purified by DEAE cellulose chromatography. This purified fraction exhibited 3 bands on SDS-PAGE compared with vicilin from other legumes which exhibite more than 3 bands generally. The results raise the possibility that the presence of the two small polypeptides in vicilin preparations is the breakdown product of the major larger one of mol.wt. 52 K and that vicilin may be a tetramer of four subunits of Mr 52000. That the high salt-soluble protein containing 52 K subunit is vicilin has been determined by several criteria.
Bhattacharyya
S P
SP
Department of Biochemistry, Bose Institute, Calcutta, India.
Biswas
B B
BB
D000596:Amino Acids / Q000032:analysis; D000645:Ammonium Sulfate; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000032:analysis; D007525:Isoelectric Focusing; D008970:Molecular Weight; D010940:Plant Proteins; D014674:Plant Proteins, Dietary / Q000737:chemistry / Q000302:isolation & purification*; D010946:Plants, Medicinal; D011487:Protein Conformation; D055314:Seed Storage Proteins; D012995:Solubility
D000596:Amino Acids; D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D055314:Seed Storage Proteins; C015575:vicilin protein, plant; D000645:Ammonium Sulfate