Blue Light Enhanced Respiratory Activity Under Photosynthetic Conditions In Chlorella; A Mass Spectrometric Analysis

1992 ◽  
Vol 47 (11-12) ◽  
pp. 881-888 ◽  
Author(s):  
Klaus P. Bader ◽  
Georg H. Schmid ◽  
Günter Ruyters ◽  
Wolfgang Kowallikb

Mass spectrometric analysis shows that blue light enhances oxygen uptake during photosynthesis in Chlorella fusca. Assays in which all of the normal 16O2 of air has been substituted by 18O2 permit discrimination between photosynthetic O2-evolution (measured as 16O2, i.e. mass 32) and O2-uptake (measured as 18O2, i.e. mass 36). A chlorophyll-free Chlorella kessleri mutant for which in earlier studies the occurrence of blue light enhanced oxidative carbohydrate degradation has been demonstrated (W. Kowallik, H. Gaffron, Planta 69, 9 2 -9 5 (1966); W. Kowallik, Ann. Rev. Plant Physiol. 33, 5 7 -7 2 (1982)) has been used for comparison in the present study. The light intensity dependencies of the observed effect seem to differ in mutant and wild type cells. In the mutant a fluence rate of 1 .5 -2 .0 (μE m -2·s-1 of blue light yields saturation, whereas in the wild type even ten times this value does not. A wavelength dependence of the effect measured with equal fluence rates at 422 nm, 457 nm, 488 nm, 555 nm and 649 nm shows maximal efficiency around 460 nm and no significant effect of red light. This agrees with earlier studies on the chlorophyll- free mutant. As a result of this correspondence, we think that the enhanced oxygen uptake during photosynthesis concerns oxidative carbohydrate degradation. The putative mechanism and significance of the observed blue light enhanced respiration in photosynthesizing Chlorella are discussed

2019 ◽  
Vol 9 (3) ◽  
pp. 161
Author(s):  
Sung-Eun Cho ◽  
Hyojin Chae ◽  
Hyung-Doo Park ◽  
Sail Chun ◽  
Yong-Wha Lee ◽  
...  

2015 ◽  
Vol 60 (6) ◽  
pp. 511-520 ◽  
Author(s):  
A.A. Efremov ◽  
◽  
V.G. Litovchenko ◽  
V.P. Melnik ◽  
O.S. Oberemok ◽  
...  

2002 ◽  
Vol 75 (3) ◽  
pp. 316 ◽  
Author(s):  
Zsolt Ablonczy ◽  
Patrice Goletz ◽  
Daniel R. Knapp ◽  
Rosalie K. Crouch

Analgesia ◽  
1995 ◽  
Vol 1 (4) ◽  
pp. 390-393 ◽  
Author(s):  
Dominic M. Desiderio ◽  
Lin Yan ◽  
Genevieve Fridland ◽  
Jih-Lie Tseng

Life ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 595
Author(s):  
Stephen Gargan ◽  
Paul Dowling ◽  
Margit Zweyer ◽  
Jens Reimann ◽  
Michael Henry ◽  
...  

Extraocular muscles (EOMs) represent a specialized type of contractile tissue with unique cellular, physiological, and biochemical properties. In Duchenne muscular dystrophy, EOMs stay functionally unaffected in the course of disease progression. Therefore, it was of interest to determine their proteomic profile in dystrophinopathy. The proteomic survey of wild type mice and the dystrophic mdx-4cv model revealed a broad spectrum of sarcomere-associated proteoforms, including components of the thick filament, thin filament, M-band and Z-disk, as well as a variety of muscle-specific markers. Interestingly, the mass spectrometric analysis revealed unusual expression levels of contractile proteins, especially isoforms of myosin heavy chain. As compared to diaphragm muscle, both proteomics and immunoblotting established isoform MyHC14 as a new potential marker in wild type EOMs, in addition to the previously identified isoforms MyHC13 and MyHC15. Comparative proteomics was employed to establish alterations in the protein expression profile between normal EOMs and dystrophin-lacking EOMs. The analysis of mdx-4cv EOMs identified elevated levels of glycolytic enzymes and molecular chaperones, as well as decreases in mitochondrial enzymes. These findings suggest a process of adaptation in dystrophin-deficient EOMs via a bioenergetic shift to more glycolytic metabolism, as well as an efficient cellular stress response in EOMs in dystrophinopathy.


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