Amaranth globulin polypeptide heterogeneity.
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 7-7.5 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 different subfamilies are interchangeable in different oligomers, some structural differences between them might affect the assembly of globulin molecules. Structural differences arising from this behavior could account for the different physicochemical properties of globulin molecules.
Quiroga
Alejandra V
AV
Centro de Investigación y Desarrollo en Criotecnología de Alimentos, Facultad de Ciencias Exactas, Universidad Nacional de La Plata y Consejo Nacional de Investigaciones Científicas y Técnicas, calle 47 y 116, 1900, La Plata, Argentina.
Martínez
E Nora
EN
Añón
M Cristina
MC
D027721:Amaranthus / Q000737:chemistry*; D015180:Electrophoresis, Gel, Two-Dimensional; D005916:Globulins / Q000737:chemistry*; D007526:Isoelectric Point; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry*; D013329:Structure-Activity Relationship
D005916:Globulins; D010940:Plant Proteins