• Proceedings of the Zoological Society Korea Conference
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• 1998.10b
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• pp.304.2-304
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• 1998

• Proceedings of the Zoological Society Korea Conference
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• 1997.10b
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• pp.231.2-231
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• 1997

No Abstract, See Full Text

• BMB Reports
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• v.40 no.5
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• pp.644-648
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• 2007

Exposure of algae or plants to irradiance from above the light saturation point of photosynthesis is known as high light stress. This high light stress induces various responses including photoinhibition of the photosynthetic apparatus. The degree of photoinhibition could be clearly determined by measuring the parameters such as absorption and fluorescence of chromoproteins. In cyanobacteria and red algae, most of the photosystem (PS) II associated light harvesting is performed by a membrane attached complex called the phycobilisome (PBS). The effects of high intensity light (1000-4000 ${\mu}mol$ photons $m^{-2}s^{-1}$) on excitation energy transfer from PBSs to PS II in a cyanobacterium Spirulina platensis were studied by measuring room temperature PC fluorescence emission spectra. High light (3000 ${\mu}mol$ photons $m^{-2}s^{-1}$) stress had a significant effect on PC fluorescence emission spectra. On the other hand, light stress induced an increase in the ratio of PC fluorescence intensity of PBS indicating that light stress inhibits excitation energy transfer from PBS to PS II. The high light treatment to 3000 ${\mu}mol$ photons $m^{-2}s^{-1}$ caused disappearance of 31.5 kDa linker polypeptide which is known to link PC discs together. In addition we observed the similar decrease in the other polypeptide contents. Our data concludes that the Spirulina cells upon light treatment causes alterations in the phycobiliproteins (PBPs) and affects the energy transfer process within the PBSs.

• ALGAE
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• v.28 no.1
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• pp.121-129
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• 2013

Intact phycobilisomes from a wild-type red Chondrus crispus and its vegetatively derived green mutant were isolated by centrifugation through a discontinuous sucrose density gradient. Pigment composition was subsequently characterized by spectrophotometry. Vegetative thalli of the two strains grown together for six months in the laboratory resulted in different pigment profiles. Two pigmented phycobilisome bands appeared in the sucrose gradient of the wild-type alga, a purple coloured one, and a pink one, whereas only a single blue band appeared in the gradient of the green mutant. Spectrophotometric and fluorescence analyses identified the phycobiliprotein composition of the purple band as the typical phycoerythrin-phycocyanin-allophycocyanin complement in the wild-type, but there was no detectable phycoerythrin present in the blue band of the green mutant. Sodium dodecyl sulphate, preparative polyacrylamide gel electrophoresis analysis confirmed the presence of allophycocyanin subunits in all extracts, but firm evidence of an R-phycoerythrin linker polypeptide in the blue band was missing. These results highlight the ability of C. crispus to adapt to a phycoerythrin deficiency by adjusting light harvesting pigment ratios.

• ALGAE
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• v.21 no.4
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• pp.479-483
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• 2006

In preparation of the biological samples for electron microscopy, the chemical fixation by glutaraldehyde, paraformaldehyde, and OsO4 has been generally used for a long time. However, the chemical fixation method has some problems: the infiltration time is a little bit long and the ultrastructure of cell or tissue transforms before complete fixation of sample. So, recently, cryo-fixation is considered more often in biomedical field. In this study, we compared High Pressure Freezing (HPF) method with chemical fixation method using a algal sample (Ptilota filicina J. Agardh), which was difficult to fix using chemical fixation method. In chloroplast, the ultrastructure of thylakoid lamella and phycobilisome can not show clearly by chemical fixation. In this study we could observe the ultrastructure of thylakoid lamella and phycobilisome of chloroplast very clearly using HPF fixation. An improved images of ultrastructures of nucleus, mitochondrion and floridean starch could obtain. These results suggest that HPF method is very useful method in algal specimen for electron microscopy.

• Plant Biotechnology Reports
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• v.4 no.3
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• pp.193-199
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• 2010

An olive-green mutant was generated in Synechocystis sp. strain PCC 6803 by inactivation of the sll0396 gene. Whole-cell absorption spectra of the mutant revealed the missing of phycocyanin peak. An investigation of the low-temperature fluorescence emission spectra revealed that the $sll0396{\Omega}$ mutant has a reduced amount of phycocyanin. Western blot analysis showed that the mutant contained less phycocyanin ${\beta}$- and ${\alpha}$-subunits and lacked the 30- and 32-kDa linker polypeptides, and northern blot analysis revealed that the transcription of the 1.4-kb cpcBA gene encoding the phycocyanin ${\beta}$- and ${\alpha}$-subunits was lower in the mutant. The Sll0396 protein has a DNA-binding motif and shares homology with known response regulators. Our results indicate that Sll0396 plays a regulatory role in the transcription of the phycocyanin genes during phycobilisome synthesis.