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...
| Authors: | , , , , |
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| Format: | article |
| Publication Date: | 2008 |
| Country: | España |
| Institution: | Universidad de Castilla-La Mancha |
| Repository: | RUIdeRA. Repositorio Institucional de la UCLM |
| OAI Identifier: | oai:ruidera.uclm.es:10578/12031 |
| Online Access: | http://hdl.handle.net/10578/12031 |
| Access Level: | Open access |
| Keyword: | Mung bean nuclease Vigna radiata Fabaceae Ribosome-inactivating protein Edman degradation |
| Summary: | 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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