Comparison of globulin proteins from Phaseolus vulgaris with those from Vicia faba

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

“…Tendergreen in the presence of SDS separated a, ,B, and y polypeptide components that differ in mol wt (3,7). agifid" .…”

“…In the cultivar Tendergreen, GI has been shown on SDS-PAGE to be composed of three protein subunits of mol wt 53,000, 47,000, and 43,000 (3,7); the subunits were called a, ,B, and -y, respectively (4). Here, further analysis of GI protein using two-dimensional electrophoresis and IEF is described and it is shown that, similar to the situation for zein, there is charge heterogeneity within each of the mol wt classes.…”

Phaseolin: Structure and Evolution

“…Phaseolin electrophoretic profiles revealed existence of three molecular weight variants of dissociated peptides termed , and [12]. The evaluation of cultivars showed three distinct patterns [15] that were named T, C and S after the cultivars Tendergreen (edible bean pods), Sanilac (dry beans) and Contender (another dry bean cultivar).…”

“…McLeester et al [12] first recognized that phaseolin can be readily precipitated by dilution from a crude acidic saline solution, thus providing a simple technique for isolating an essentially pure form of the protein. The ability to obtain large quantities of purified phaseolin facilitated electrophoretic studies using one dimensional SDS gels [12] and characterization by equilibrium sedimentation [13].…”

“…The ability to obtain large quantities of purified phaseolin facilitated electrophoretic studies using one dimensional SDS gels [12] and characterization by equilibrium sedimentation [13]. These initial forays paved the way for biophysical characterization [14][15][16][17] and the subsequent crystallographic structural analysis [18][19][20][21].…”