scholarly journals The separation of photochemically active PS-I and PS-II containing chlorophyll-protein complexes by isoelectric focusing of bean thylakoids on polyacrylamide gel plates

FEBS Letters ◽  
1979 ◽  
Vol 104 (1) ◽  
pp. 71-77 ◽  
Author(s):  
Dorothea Siefermann-Harms ◽  
Helga Ninnemann
1980 ◽  
Vol 35 (7-8) ◽  
pp. 627-637 ◽  
Author(s):  
Aloysius Wild ◽  
Barbara Urschel

Chlorophyll-protein complexes from thylakoids of the normal type and two mutants of Chlorella fusca were separated using sodium dodecyl sulfate acrylamide gel electrophoresis (PAGE). The properties of the chlorophyll-protein complexes of the three strains of Chlorella were compared. Standard curves were set up for the characterization of the chlorophyll-proteins. In every electrophoretic separation of chlorophyll-protein complexes, a certain amount of pigment is separated from the protein. We tried to keep that amount as low as possible by mild solubiliza­tion and by working in low temperature. Under these conditions, we obtained several new chlorophyll-proteins in addition to the P-700-chlorophyll a-protein (CP I) and the light-harvesting chlorophyll a/b-protein (CP II). Thus, a small band (CP I a) was located between the top of the gel and the CPI after elec­trophoresis. Although it shows spectral qualities similar to CP I, it possesses a much lower chloro­phyll a/chlorophyll b ratio. It may be an aggregate of photosystem I and light-harvesting chloro­phyll. We found and analyzed three other chlorophyll-proteins with electrophoretic mobilities inter­mediate between that of the P-700-chlorophyll a-protein and that of the light-harvesting chloro­phyll a/b-protein complex. Two of these chlorophyll-proteins, the LHCP1 and the LHCP2, have a low chlorophyll a/chlorophyll b ratio and spectral properties similar to that of the light-harvesting chlorophyll a/b-protein (LHCP3). They obviously represent dimers or oligomers of the latter com­plex. A third, new complex (CPa) migrated between LHCP3 and its dimer. With the chlorophyll b deficient mutant G 36 of Chlorella fusca, this complex could be obtained in high purity and great enrichment (15% of total chlorophyll). It could be proved that this complex only contains chloro­phyll a. Its red absorption maximum is at 671 nm. Some indirect evidences suggest that it may be a good candidate for the PS II reaction center complex.


1982 ◽  
Vol 202 (1) ◽  
pp. 25-29 ◽  
Author(s):  
R P F Gregory ◽  
G Borbély ◽  
S Demeter ◽  
A Faludi-Dániel

Circular dichroism (c.d.) was measured for four chlorophyll-protein complexes, resolved from sodium dodecyl sulphate extracts of chloroplasts by electrophoresis in polyacrylamide gel containing Deriphat 160 (disodium N-dodecyl beta-imidopropionate), a zwitterionic detergent. The slowest-band (1) complex was found to be identical with the complex CP1 as found on electrophoresis in the presence of anion detergent, but it was in a much higher yield (30% of the chlorophyll a). In band-2 and -3 protein complexes a c.d. pattern described for the complex CP2 could be recognized. Another c.d. component of a split-exciton type with extrema at 680 (-) and 669 (+)nm, together with evidence of disorganized chlorophyll, was found in band-2, -3 and -4 complexes. When a barley (Hordeum vulgare) mutant lacking chlorophyll b was examined, only bands 1 and 4 were obtained, and the c.d. of the band-4 complex was much less affected by disorganized chlorophyll. C.D. spectra resembling that of this band-4 complex could be generated by subtracting the c.d. of complex CP1 from the c.d. of photochemically active mutant chloroplast fragments, or by subtracting the c.d. of complexes CP1 and CP2 from pea (Pisum sativum) chloroplast fragments. The Deriphat appears to have preserved at least to some extent a new type of chlorophyll a-protein complex.


2002 ◽  
Vol 75 (6) ◽  
pp. 613 ◽  
Author(s):  
Stefano Santabarbara ◽  
Ilaria Cazzalini ◽  
Andrea Rivadossi ◽  
Flavio M. Garlaschi ◽  
Giuseppe Zucchelli ◽  
...  

1982 ◽  
Vol 37 (3-4) ◽  
pp. 256-259 ◽  
Author(s):  
F. Schuler ◽  
P. Brandt ◽  
W. Wießner

Abstract An improved method for isolation of (photosystem II)-particles from Euglena gracilis, strain Z was established. PS II-particles isolated by ultrasonic treatment and following differential centrifugation show fluorescence emission and absorption spectra identical with in vivo properties of Euglena gracilis. These PS II-particles have only PS II-activity and contain CP a, the typical chlorophyll-protein-complex of PS II. No contamination of PS I-components are detectable.


2021 ◽  
Author(s):  
Tingting Chen ◽  
Yu Sheng ◽  
Zhaodong Hao ◽  
Xiaofei Long ◽  
Fangfang Fu ◽  
...  

Abstract Polyploidy generally provides an advantage in phenotypic variation and growth vigor. However, the underlying mechanisms remain poorly understood. The tetraploid L. sino-americanum exhibits altered morphology compared to its diploid counterpart, including larger, thicker and deeper green leaves, bigger stomata, thicker stems and increased tree height. Such characteristics can be useful in ornamental and industrial applications. To elucidate the molecular mechanisms behind this variation, we performed a comparative transcriptome and proteome analysis. Our transcriptome data indicated that some photosynthesis genes and pathways were differentially altered and enriched in tetraploid L. sino-americanum, mainly related to F-type ATPase, the cytochrome b6/f complex, photosynthetic electron transport, the light harvesting chlorophyll protein complexes, photosystem I and II. Most of the differentially expressed proteins we could identify are also involved in photosynthesis. Our physiological results showed that tetraploids have an enhanced photosynthetic capacity, concomitant with great levels of sugar and starch in leaves. This suggests that tetraploid L. sino-americanum might experience comprehensive transcriptome reprogramming of genes related to photosynthesis. This study has especially emphasized molecular changes involved in photosynthesis that accompany polyploidy, and provides a possible explanation for the altered phenotype of polyploidy plants in comparison to their diploid form.


2021 ◽  
Vol 68 (5) ◽  
pp. 867-872
Author(s):  
M. S. Khristin ◽  
T. N. Smolova ◽  
V. D. Kreslavski

Abstract The dynamics of changes in the photochemical activity of photosystem II (PSII) and low-temperature spectra at 77 K in the first leaves of 11-day winter wheat plants Triticum aestivum L., as well as structural changes in chlorophyll-protein complexes (CPC) of thylakoid membranes during recovery after a short-term (20 min) heating at a temperature of 42°C, were studied. Changes in the Fv/Fm, F735/F695, and F735/F685 ratios indicate inhibition of PSII immediately after heating. Using nondenaturing electrophoresis, it was shown that the light-harvesting Chl a/b complex of PSII does not aggregate immediately after heating but after several hours, after 6 h the desagregation of CPC was observed, which was consistent with an increase in the Fv/Fm ratio upon recovery. The influence of temperature, intensity, and quality of light (white, blue, and red light) on the recovery of PSII activity and low-temperature fluorescence spectra was studied. It was concluded that the recovery is a photo-activated low-energy process, independent of photosynthesis, and the most effective in blue light.


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