Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
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 m...
| Autores: | , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2000 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/113475 |
| Acceso en línea: | http://hdl.handle.net/11336/113475 |
| Access Level: | acceso abierto |
| Palabra clave: | Amaranth Globulin Papain Protein structure Proteolysis https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| Sumario: | 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. |
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