Microheterogeneity of Globulin-1 Storage Protein from French Bean with Isoelectrofocusing
Authors:
- John W. S. BrownJBJohn W. S. Brown
- Fredrick A. BlissFBFredrick A. Bliss
- Timothy C. HallTHTimothy C. Hall
- 1 November 1980
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 66 (5) , 838-840
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.Keywords
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