Amaranth Globulin Polypeptide Heterogeneity
- Quiroga, Alejandra Viviana
- Martinez, Estela Nora
- Añon, Maria Cristina
DOIAbstract
The polypeptides integrating amaranth globulin-p and 11S-globulin were characterized by two-dimensional electrophoresis, ion-exchange chromatography and RP-HPLC. All polypeptides exhibited charge and hydrophobic heterogeneity. Almost all acid (A, pI 5 - 7) and basic (B, pI 9 - 10) polypeptides were present in both globulins, and the same happened with the unprocessed M polypeptides with pI in the range of 7 to 7.5 which fits well with a sequence containing both the A and B polypeptides. There were other polypeptides only present in 11S-globulin, like some of 41 and 16 kDa which might come from another precursor or be the products of a different processing of the propolypeptide. These results suggested that, although amaranth subunits from d...
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