N-Terminal Amino Acid Sequences of Intact and Cleaved Forms of Mung Bean Nuclease
We report, for the first time, the N-terminal amino acid sequences of both intact and cleaved forms (fragments A and B) of Mung bean nuclease, purified from sprouts of Vigna radiata or purchased from Amersham Biosciences. The N-terminal sequence of Mung bean nuclease shows high similarity with the p...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2008 |
| País: | España |
| Institución: | Universidad de Castilla-La Mancha |
| Repositorio: | RUIdeRA. Repositorio Institucional de la UCLM |
| OAI Identifier: | oai:ruidera.uclm.es:10578/12031 |
| Acceso en línea: | http://hdl.handle.net/10578/12031 |
| Access Level: | acceso abierto |
| Palabra clave: | Mung bean nuclease Vigna radiata Fabaceae Ribosome-inactivating protein Edman degradation |
| Sumario: | We report, for the first time, the N-terminal amino acid sequences of both intact and cleaved forms (fragments A and B) of Mung bean nuclease, purified from sprouts of Vigna radiata or purchased from Amersham Biosciences. The N-terminal sequence of Mung bean nuclease shows high similarity with the putative bifunctional nuclease from Arabidopsis thaliana (AC: AAM63596). |
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