Partial purification of cell wall α‐galactosidases and α‐arabinosidases from Cicer arietinum epicotyls. Relationship with cell wall autolytic processes
Two protein fractions with activity as a-galactosidase (EC 3.2.1.22) and a-arabinosidase (EC 3.2.1.55), respectively, were identified in the proteins of cell wall of Cicer arietinum L. cv. Castellana extracted with 3 M LiCI. These fractions were partially purified by gel filtration chromatography (...
| Autores: | , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 1989 |
| País: | España |
| Institución: | Universidad de Salamanca (USAL) |
| Repositorio: | GREDOS. Repositorio Institucional de la Universidad de Salamanca |
| OAI Identifier: | oai:gredos.usal.es:10366/157393 |
| Acceso en línea: | http://hdl.handle.net/10366/157393 |
| Access Level: | acceso embargado |
| Palabra clave: | a-arabinosidase Cell wall Cicer arietinum Epicotyls a-galactosidase Glucanase |
| Sumario: | Two protein fractions with activity as a-galactosidase (EC 3.2.1.22) and a-arabinosidase (EC 3.2.1.55), respectively, were identified in the proteins of cell wall of Cicer arietinum L. cv. Castellana extracted with 3 M LiCI. These fractions were partially purified by gel filtration chromatography (Bio Gel P-150), increasing the specific arabinosidase activity 57-fold and the a-galactosidase activity 6-fold. Other protein fractions with glucosidase (EC 3.2.1.21) and glucanase (EC 3.2.1.6) activity also appeared. According to earlier authors, a-arabinosidases and a-galactosidases are related to alterations in linkages occurring in cell walls, since the enzymes are able to hydrolyze isolated wall polymers. However, our preparations hydrolyze intact cell walls only to a very limited extent, such that their participation in the autolytic processes of cell walls can be ruled out. |
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