Cereal Chem 58:92 - 96.  |  VIEW ARTICLE
Physical and Hydrodynamic Studies on Salt-Soluble Proteins of Mungbean.

A. S. Narang, G. S. Bains, and I. S. Bhatia. Copyright 1981 by the American Association of Cereal Chemists, Inc. 

Proteins were isolated from salt-soluble mungbean (Phaseolus aureus), variety 54. Gel filtration showed the proteins to be homogeneous, having a molecular weight of 62,500, a Stokes' radius of 33 angstroms, and pI of 5.85. The presence of two fractions was suspected from the starch gel electrophoresis. Partial specific volume, intrinsic viscosity, kinematic viscosity, voluminosity, conformation, and polarity ratios were determined. These proteins were spherical, with a radius of 25 angstroms, and had a water shell 8 angstroms thick, corresponding to about three layers of water molecules. Their conformation was stable in the temperature range 35-85 C. About 36% of the polar residues were on the surface of the protein.