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).
N-terminal amino acid sequences of intact and cleaved forms of mung bean nuclease.
DELLI BOVI, PASQUALE;
2008
Abstract
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).File in questo prodotto:
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