1,721,062 research outputs found
MODULATORY EFFECT OF TWO CARDIOGLYCOSIDES ON RECONSTITUTED Na-K ATPase IN PROTEOLIPOSOMES
Caratterizzazione proteomica delle risposte allo stress indotto dal rame in radici di Cannabis sativa L.
Proteomic approach for evaluating copper stress in Cannabis sativa roots mycorrhized and non-mycorrhized by Glomus intraradices.
OXIDATIVE ALCOHOL DEHYDROGENASE (ADH2) FROM KLUYVEROMYCES MARXIANUS CULTURES IN DOUBLE STEP SUBSTRATE MEDIA
Improved resistance to transition metals of a cobalt-substituted alcohol dehydrogenase 1 from saccharomyces cerevisiae
The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases
Enzymatic reduction of arsenate to arsenite is the first known step in arsenate metabolism in all organisms. Although the presence of one mRNA arsenate reductase (PvACR2) has been characterized in gametophytes of P. vittata, no arsenate reductase protein has been directly observed in this arsenic hyperaccumulating fern, yet. In order to assess the possible presence of arsenate reductase in P. vittata, two recombinant proteins, ACR2-His6 and Trx-His6-S-Pv2.5-8 were prepared in Escherichia coli, purified and used to produce polyclonal antibodies. The presence of these two enzymes was evaluated by qRT-PCR, immunoblotting and direct MS analysis. Enzymatic activity was detected in crude extracts. For the first time we detected and identified two arsenate reductase proteins (PvACR2 and Pv2.5-8) in sporophytes and gametophytes of P. vittata. Despite an increase of the mRNA levels for both proteins in roots, no difference was observed at the protein level after arsenic treatment. Overall, our data demonstrate the constitutive protein expression of PvACR2 and Pv2.5-8 in P. vittata tissues and propose their specific role in the complex metabolic network of arsenic reduction
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