Linked Life Data

2574469

Source:http://linkedlifedata.com/resource/pubmed/id/2574469

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pubmed-article:2574469pubmed:abstractTextBased 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.lld:pubmed
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pubmed-article:2574469pubmed:authorpubmed-author:TrenchR KRKlld:pubmed
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pubmed-article:2574469pubmed:pagination53-72lld:pubmed
pubmed-article:2574469pubmed:dateRevised2010-11-18lld:pubmed
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pubmed-article:2574469pubmed:articleTitleThe biogenesis of the cyanellae of Cyanophora paradoxa. I. Polypeptide composition of the cyanellae.lld:pubmed
pubmed-article:2574469pubmed:affiliationDepartment of Biological Sciences, University of California, Santa Barbara 93106.lld:pubmed
pubmed-article:2574469pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2574469pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:2574469pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed