scholarly journals expression of a taste-modifying protein, miraculin, in by-2 tobacco cell line (Nicotiana tabacum L. Cv Bright Yellow 2)

2015 ◽  
Vol 36 (3) ◽  
Author(s):  
La Viet Hong ◽  
Nguyen Thu Giang ◽  
Pham Bich Ngoc ◽  
Chu Hoang Ha
Molecules ◽  
2018 ◽  
Vol 23 (12) ◽  
pp. 3179 ◽  
Author(s):  
Peng Zhang ◽  
Xin Li ◽  
Xiao-Long Yuan ◽  
Yong-Mei Du ◽  
Bin-Gui Wang ◽  
...  

An endophytic fungus Arthrinium arundinis TE-3 was isolated and purified from the fresh leaves of cultivated tobacco (Nicotiana tabacum L.). Chemical investigation on this fungal strain afforded three new prenylated diphenyl ethers (1−3) as well as three known analogues (4−6). Structure elucidation of the isolated compounds was carried out by analysis of 1D and 2D nuclear magnetic resonance (NMR) and high-resolution electrospray ionization mass spectroscopy (HRESIMS) spectra, as well as by comparison of those data with literature data. The absolute configuration of the stereogenic center at C-8 in 1 was assigned by comparison of the experimental and calculated ECD spectra. Compounds 1 and 2 showed selective antifungal activity against Mucor hiemalis with minimum inhibitory concentration (MIC) values of 8 and 4 μg/mL, respectively. Compounds 5 and 6 exhibited inhibitory activity against Alteraria alternata with an MIC value of 8 μg/mL. In the cytotoxic assay, 2, 5, and 6 displayed moderate in vitro cytotoxicity against the human monocytic cell line (THP-1 cell line), with IC50 values of 40.2, 28.3, and 25.9 μM, respectively. This study indicated that endophytic fungi possess great potential for exploring new bioactive secondary metabolites.


2005 ◽  
Vol 0 (0) ◽  
pp. 051020045109001-???
Author(s):  
Akihiro Saito ◽  
Kyoko Higuchi ◽  
Midori Hirai ◽  
Rie Nakane ◽  
Masaaki Yoshiba ◽  
...  

1987 ◽  
Vol 5 (2) ◽  
pp. 155-164
Author(s):  
Francisco A. Culi��ez-maci� ◽  
Eduardo Primo-Millo ◽  
Jos� Hern�ndez-Yago ◽  
Jos� Guerri-Sirera ◽  
Eduardo Primo-Y�fera

PROTOPLASMA ◽  
2003 ◽  
Vol 221 (1-2) ◽  
pp. 93-100 ◽  
Author(s):  
T. Raeymaekers ◽  
G. Potters ◽  
H. Asard ◽  
Y. Guisez ◽  
N. Horemans

2005 ◽  
Vol 389 (3) ◽  
pp. 695-704 ◽  
Author(s):  
Sandra Matic ◽  
Daniela A. Geisler ◽  
Ian M. Møller ◽  
Susanne Widell ◽  
Allan G. Rasmusson

The ion channel-forming peptide AlaM (alamethicin) is known to permeabilize isolated mitochondria as well as animal cells. When intact tobacco (Nicotiana tabacum L.) Bright Yellow-2 cells were treated with AlaM, the cells became permeable for low-molecular-mass molecules as shown by induced leakage of NAD(P)+. After the addition of cofactors and substrates, activities of cytosolic as well as mitochondrial respiratory enzymes could be directly determined inside the permeabilized cells. However, at an AlaM concentration at which the cytoplasmic enzymes were maximally accessible, the vacuole remained intact, as indicated by an unaffected tonoplast proton gradient. Low-flux permeabilization of plasma membranes and mitochondria at moderate AlaM concentrations was reversible and did not affect cell vigour. Higher AlaM concentrations induced cell death. After the addition of catalase that removes the H2O2 necessary for NADH oxidation by apoplastic peroxidases, mitochondrial oxygen consumption could be measured in permeabilized cells. Inhibitor-sensitive oxidation of the respiratory substrates succinate, malate and NADH was observed after the addition of the appropriate coenzymes (ATP, NAD+). The capacities of different pathways in the respiratory electron-transport chain could thus be determined directly. We conclude that AlaM permeabilization provides a very useful tool for monitoring metabolic pathways or individual enzymes in their native proteinaceous environment with controlled cofactor concentrations. Possible uses and limitations of this method for plant cell research are discussed.


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