Identification of a Mitochondrial Nucleoside Diphosphate Kinase from the Green Alga Dunaliella tertiolecta
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چکیده
منابع مشابه
Isolation of Intact Chloroplasts from Dunaliella tertiolecta.
Cells of Dunaliella tertiolecta from the log phase of growth were broken by rapid extrusion at low pressure through a Yeda press and the chloroplasts were isolated by centrifugation through a Percoll gradient. Osmolarity of the growth media, the suspending media, and the Percoll gradient was kept identical to minimize change in chloroplast volume and mitochondrial entrapment. The isolated intac...
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Nucleoside diphosphate (NDP) kinase from Escherichia coli was purified to homogeneity and was crystallized. Gel filtration analysis of the purified enzyme indicated that it forms a tetramer. The enzyme was phosphorylated with [gamma-32P]ATP, and the pH stability profile of the phosphoenzyme indicated that two different amino acid residues were phosphorylated. Both a histidine residue and serine...
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The variation of the lipophilic (carotenoids and α-tocopherol) and hydrophilic (glutathione and ascorbic acid) antioxidant contents, and the activities of antioxidant enzyme such superoxide dismutase (SOD), catalase (CAT) and peroxidase (POD), as well as cellular malonaldehyde and stable radicals of D. salina in response to ultraviolet B (UV-B radiation 290-320 nm) and secondary carotenoid indu...
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We identify four novel DNA-binding complexes in the nuclear-encoded Lhcb1 promoter of the chlorophyte alga Dunaliella tertiolecta that are regulated by photosynthetic pathways in the plastid. The binding activities of three of the complexes were positively correlated with time-dependent changes in Lhcb1 transcript abundance, implicating their roles as transcriptional enhancers in a retrograde s...
متن کاملPartial purification and characterization of a Ca(2+)-dependent protein kinase from the green alga, Dunaliella salina.
A calcium-dependent protein kinase was partially purified and characterized from the green alga Dunaliella salina. The enzyme was activated at free Ca2+ concentrations above 10(-7) molar. and half-maximal activation was at about 3 x 10(-7) molar. The optimum pH for its Ca(2+)-dependent activity was 7.5. The addition of various phospholipids and diolein had no effects on enzyme activity and d...
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ژورنال
عنوان ژورنال: Plant and Cell Physiology
سال: 2002
ISSN: 1471-9053,0032-0781
DOI: 10.1093/pcp/pcf155