Microheterogeneity of Globulin-1 Storage Protein from French Bean with Isoelectrofocusing

Abstract
The major storage protein fraction, globulin-1 protein, of French bean (Phaseolus vulgaris L.) was analyzed by 2-dimensional electrophoresis. The protein pattern suggested a more complex system for globulin-1 protein than the model of 3 polypeptides, .alpha., .beta. and .gamma., differing in MW. Isoelectrofocusing analyses of the individual proteins showed that each exhibited charge microheterogeneity over a similar pH range. Isoelectrofocusing banding patterns may help to understand the relationships between the globulin-1 polypeptide subunits.