Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
- Castellani, Oscar Francisco
- Martinez, Estela Nora
- Añon, Maria Cristina
DOIAbstract
Globulin-P was partially hydrolyzed with papain under specific conditions to study the resulting structural modifications. Under mild hydrolytic conditions, globulin-P polymers were cleaved to render their unitary constituents (280 kDa molecules). Under stronger hydrolytic conditions these unitary molecules were 13% smaller than those from nonhydrolyzed globulin. Moreover, these molecules remained assembled even though they contained degraded polypeptides. The monomeric (M) subunit and the A chains were preferentially cleaved under mild and intermediate hydrolytic conditions, whereas B chains remained with the same size. These results suggest that the M and A polypeptides might be located at an exposed site of the molecules resembling the s...
_(cropped).jpg%3Fwidth%3D300&w=3840&q=75)
Add to ORKG