Longitudinal Profiles of Growth, Photosynthesis and Light Independent Carbon Fixation in the Antarctic Brown Alga Ascoseira mirabilis

1995 ◽  
Vol 38 (1-6) ◽  
Author(s):  
I. Gómez ◽  
D. N. Thomas ◽  
C. Wiencke
2020 ◽  
pp. 1-5
Author(s):  
Leandro da Costa Clementino ◽  
Fernando Bombarda Oda ◽  
Thaiz Rodrigues Teixeira ◽  
Renata Spagolla Napoleão Tavares ◽  
Pio Colepicolo ◽  
...  

2020 ◽  
Vol 185 ◽  
pp. 102347
Author(s):  
Bo Wang ◽  
Min Chen ◽  
Feng Chen ◽  
Renming Jia ◽  
Xiaopeng Li ◽  
...  

1990 ◽  
Vol 33 (3) ◽  
pp. 251-256 ◽  
Author(s):  
D. G. Müller ◽  
R. Westermeier ◽  
A. Peters ◽  
W. Boland

2020 ◽  
Vol 63 (6) ◽  
pp. 541-549
Author(s):  
Chenlin Liu ◽  
Xiuliang Wang

AbstractThe Antarctic endemic brown alga Ascoseira mirabilis is physically and physiologically well adapted to the extreme polar environment. To better understand the molecular strategies associated with stress adaptation, the transcriptome of A. mirabilis was sequenced, and its antioxidant enzyme genes were identified and compared with other algae. A total of 126,576 unigenes with a mean length of 734 bp and N50 of 1174 bp was assembled from the transcriptome data. Phylogenetic analysis revealed that dramatic evolutionary changes had occurred in the brown algal superoxide dismutases (SODs) and class I peroxidases that were not consistent with the phylogeny of the species. Fe/Mn SODs are more prevalent in brown algae than in red and green algae. Two additional Fe-SODs in A. mirabilis were phylogenetically closely related to those of green algae, but not to those in other brown algae. We also identified three A. mirabilis ascorbate peroxidase (APx) genes that had a different origin from other brown algal APxs. The SOD and APx genes specifically identified in A. mirabilis will be crucial for understanding the evolution of the algal antioxidant enzymes that contribute to ecological success under extreme environmental conditions in the Antarctic region.


Author(s):  
Gunnel Karlsson ◽  
Jan-Olov Bovin ◽  
Michael Bosma

RuBisCO (D-ribulose-l,5-biphosphate carboxylase/oxygenase) is the most aboundant enzyme in the plant cell and it catalyses the key carboxylation reaction of photosynthetic carbon fixation, but also the competing oxygenase reaction of photorespiation. In vitro crystallized RuBisCO has been studied earlier but this investigation concerns in vivo existance of RuBisCO crystals in anthers and leaves ofsugarbeets. For the identification of in vivo protein crystals it is important to be able to determinethe unit cell of cytochemically identified crystals in the same image. In order to obtain the best combination of optimal contrast and resolution we have studied different staining and electron accelerating voltages. It is known that embedding and sectioning can cause deformation and obscure the unit cell parameters.


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