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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1290
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pubmed:dateCreated |
1990-1-24
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pubmed:abstractText |
Based on polypeptide separation, protein purification and immunoblotting techniques using heterologous antibodies, we have been able to identify several photosynthetically important polypeptide components of the cyanellae of Cyanophora paradoxa. Cytochrome c-552 and ferredoxin have been purified to electrophoretic homogeneity and exhibit apparent molecular masses of 10.5 and 9.0 kDa, respectively. Cytochrome c-552 has an isoelectric point of pH 4.2 +/- 0.1. Plastocyanin was immunologically and spectrally undetectable even in cells grown in the presence of Cu2+. Polypeptides for cytochromes f, b-6 and c-552 have been located in electrophoretically resolved thylakoid samples by using the TMBZ-staining procedure. Intact phycobilisomes have been purified and characterized with respect to polypeptide composition and absorption and emission spectra. Photosystems I and II have been isolated and characterized with respect to their photochemical activities, spectral characteristics and polypeptide composition. Photochemically active PS I complexes fluoresce maximally at 720 nm at 77 K and comprise five polypeptide subunits resolved under denaturing conditions with apparent molecular masses of 66, 21, 18, 14 and 11 kDa. PS II core complexes mediate light-dependent 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU)-sensitive electron transfer between 1,5-diphenylcarbazide (DPC) and 2,6-dichlorophenolindophenol (DPIP) at rates of 140-200 mumol h-1 mg-1 chlorophyll. These complexes exhibit absorption maxima at 436 and 673 nm and show fluorescence emission maxima at 685 and 695 nm at 77 K. Rubisco was separated by two-dimensional electrophoresis and immunologically characterized.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chlorophyll,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Light-Harvesting Protein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/Phycobilisomes,
http://linkedlifedata.com/resource/pubmed/chemical/Pigments, Biological,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome C-552,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome c553
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0080-4649
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
238
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
53-72
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2574469-Cell Fractionation,
pubmed-meshheading:2574469-Chlorophyll,
pubmed-meshheading:2574469-Cytochrome c Group,
pubmed-meshheading:2574469-Electron Transport,
pubmed-meshheading:2574469-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2574469-Eukaryota,
pubmed-meshheading:2574469-Immunoblotting,
pubmed-meshheading:2574469-Light-Harvesting Protein Complexes,
pubmed-meshheading:2574469-Molecular Weight,
pubmed-meshheading:2574469-Organelles,
pubmed-meshheading:2574469-Peptide Biosynthesis,
pubmed-meshheading:2574469-Peptides,
pubmed-meshheading:2574469-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:2574469-Phycobilisomes,
pubmed-meshheading:2574469-Pigments, Biological,
pubmed-meshheading:2574469-Plant Proteins
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pubmed:year |
1989
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pubmed:articleTitle |
The biogenesis of the cyanellae of Cyanophora paradoxa. I. Polypeptide composition of the cyanellae.
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pubmed:affiliation |
Department of Biological Sciences, University of California, Santa Barbara 93106.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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