Membrane polypeptides and chlorophyll–protein complexes of maize mesophyll chloroplasts

1976 ◽  
Vol 54 (14) ◽  
pp. 1684-1689 ◽  
Author(s):  
D. B. Hayden ◽  
W. G. Hopkins
Keyword(s):  
Chlorophyll A ◽  
Gel Electrophoresis ◽  
Protein Complexes ◽  
Molecular Weights ◽  
Chlorophylls A And B ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

Polypeptide profiles of maize mesophyll chloroplast lamellae have been obtained using SDS – acrylamide gel electrophoresis. Molecular weights have been assigned to the major polypeptides using the same technique. Chlorophyll–protein complexes from lamellae have been resolved using both SDS – acrylamide gel electrophoresis and chromatography on hydroxylapatite. Chlorophyll a alone is associated with a 69-kilodalton polypeptide while both chlorophylls a and b are associated with a 23-kilodalton component.

Partition of Phylloquinone Kx between Digitonin Particles and Chlorophyll-Proteins of Chloroplast Membranes from Nicotiana tabacum

1981 ◽  
Vol 36 (3-4) ◽  
pp. 276-283 ◽  
Author(s):  
E. Interschick-Niebler ◽  
H. K. Lichtenthaler
Keyword(s):  
Nicotiana Tabacum ◽  
Photosystem Ii ◽  
Chlorophyll A ◽  
Gel Electrophoresis ◽  
Protein Complexes ◽  
Sodium Dodecylsulfate ◽  
Total Chlorophyll ◽  
Photosynthetic Membrane ◽  
Chlorophylls A And B ◽  
Β Carotene

The partition of phylloquinone (vitamin K1), of chlorophylls a and b and of the two main carotenoids, β-carotene and lutein, in subthylakoid particles (digitonin treatment) and chlorophyll protein complexes (sodium dodecylsulfate polyamide-gel electrophoresis) isolated from tobacco chloroplasts (Nicotiana tabacum L.) is described. 1. The “light particle” fractions (S 90 000, S 150 000) of digitonin fragmented chloroplasts are enriched in CP I and contain a higher proportion of phylloquinone, chorophyll a and β-carotene as compared to whole chloroplasts. This is visualized by high values for the ratio a/b (6 -8) and for β-carotene/lutein (1.7) as well as about 3 mol of K1 per 100 mol of total chlorophyll. The “heavy digitonin particle” fraction (10 000 x g sediment), in turn, contains a higher proportion of chlorophyll b and lutein, but a lower level of phylloquinone than whole chloroplasts. 2. The chlorophyll a-protein CP I of pigmentsystem I, isolated by preparative gel electrophoresis using 0.5% and 4% SDS, is characterized by a stable level of phylloquinone (1 mol K1 per 100 mol of total chlorophyll), high chlorophyll a/b ratios (7 -10) and high values for β-carotene/lutein (~ 6.0). The light-harvesting chlorophyll a/b-protein LHCP of photosystem II (chlorophyll a/b = 1.1 - 1.5, β-carotene/lutein = < 0.1) contains either low amounts of phylloquinone (0.5% SDS) or only trace amounts of K1 (4% SDS). The free pigment fraction (FP) contains at 0.5% SDS 57% of the total phylloquinone of thylakoid membranes. At 4% SDS the K1 amount in the free pigment fraction increases to 84%. 3. The phylloquinone partition studies in digitonin particles and SDS chlorophyll proteins indicate that there exist at least two localization sites for phylloquinone K1 in the photosynthetic membrane. The CP I complex and a second site, presumably near photosystem II (CPa?)

Chlorophyll-Protein Complexes of Chlorella fusca

1980 ◽  
Vol 35 (7-8) ◽  
pp. 627-637 ◽  
Author(s):  
Aloysius Wild ◽  
Barbara Urschel
Keyword(s):  
Chlorophyll A ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Sodium Dodecyl ◽  
Chlorophyll B ◽  
Chlorella Fusca ◽  
Ps Ii ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Set Up

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.

scholarly journals Chiroptical properties of chlorophyll-protein complexes separated on Deriphat/polyacrylamide gel

1982 ◽  
Vol 202 (1) ◽  
pp. 25-29 ◽  
Author(s):  
R P F Gregory ◽  
G Borbély ◽  
S Demeter ◽  
A Faludi-Dániel
Keyword(s):  
Chlorophyll A ◽  
Protein Complexes ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Chlorophyll B ◽  
Chlorophyll Protein Complexes ◽  
New Type ◽  
Chlorophyll Protein ◽  
Zwitterionic Detergent ◽  
Exciton Type

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.

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