INVESTIGADORES
AÑON Maria Cristina
artículos
Título:
Amaranth globulins: structure modifications induced by enzymatic proteolysis
Autor/es:
CASTELLANI, O.F; MARTINEZ, E.N; AÑÓN, M.C
Revista:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Editorial:
AMER CHEMICAL SOC
Referencias:
Año: 2000 vol. 48 p. 5624 - 5629
ISSN:
0021-8561
Resumen:
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 structure of the
legumins. The M subunit may be participating in the stabilization of globulin-P polymers, on the
basis that these two species disappeared under the same hydrolytic conditions. Similar events such
as those described in this paper might be taking place on globulin-P during germination of amaranth
grain.