Molecular weight determination of an active photosystem I preparation from a thermophilic cyanobacterium, Synechococcus elongatus

An active photosystem I (PSI) complex was isolated from the thermophilic cyanobacterium Synechococcus elongatus by a procedure consisting of three steps: First, extraction of photosystem II from the thylakoids by a sulfobetaine detergent yields PSI-enriched membranes. Second, the latter are treated...

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Bibliographic Details
Published in:Biochemistry (Easton) 1990-02, Vol.29 (5), p.1216-1225
Main Authors: Schafheutle, Monika E, Setlikova, Eva, Timmins, Peter A, Johner, Herbert, Gutgesell, Peter, Welte, Wolfram, Setlik, Ivan
Format: Article
Language:English
Subjects:
AMINO ACIDS
Amino Acids - analysis
BARYONS
BASIC BIOLOGICAL SCIENCES
CARBOXYLIC ACIDS
Cell Membrane - analysis
CHEMICAL ANALYSIS
CHLOROPHYLL
Chlorophyll - analysis
CHROMATOGRAPHY
CYANOBACTERIA
Cyanobacteria - analysis
ELECTRON MICROPROBE ANALYSIS
Electron Probe Microanalysis
ELEMENTARY PARTICLES
FERMIONS
HADRONS
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
ION EXCHANGE CHROMATOGRAPHY
Light-Harvesting Protein Complexes
MICROANALYSIS
MICROORGANISMS
MOLECULAR WEIGHT
NEUTRONS
NUCLEONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
Photosynthetic Reaction Center Complex Proteins
PHOTOSYNTHETIC REACTION CENTERS
photosystem I
Photosystem I Protein Complex
Photosystem II Protein Complex
Phycobilisomes
PHYTOCHROMES
PIGMENTS
Plant Proteins - analysis
PORPHYRINS
PROTEINS
SEPARATION PROCESSES 550201 > Biochemistry-- Tracer Techniques
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Summary:An active photosystem I (PSI) complex was isolated from the thermophilic cyanobacterium Synechococcus elongatus by a procedure consisting of three steps: First, extraction of photosystem II from the thylakoids by a sulfobetaine detergent yields PSI-enriched membranes. Second, the latter are treated with Triton X-100 to extract PSI particles, which are further purified by preparative isoelectric focusing. Third, anion-exchange chromatography is used to remove contaminating phycobilisome polypeptides. The purified particles show three major bands in sodium dodecyl sulfate gel electrophoresis of apparent molecular mass of 110, 15, and 10 kDa. Charge separation was monitored by the kinetics of flash-induced absorption changes at 820 nm. A chlorophyll/P700 ratio of 60 was found. When the particles are stored at 4 degrees C, charge separation was stable for weeks. The molecular mass of the PSI particles, determined by measurement of zero-angle neutron scattering intensity, was 217,000 Da. The PSI particles thus consist of one heterodimer of the 60-80-kDa polypeptides and presumably one copy of the 15- and 10-kDa polypeptides, respectively.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00457a018