Formation of truncated proteins and high-molecular-mass aggregates upon soft illumination of photosynthetic proteins

Journal of Proteome Research

Volumn 4, Issue 6, 2005, Pages 2327-2337

  Rinalducci, Sara ^a   Campostrini, Natascia ^b   Antonioli, Paolo ^b   Righetti, Pier Giorgio ^b,c   Roepstorff, Peter ^d   Zolla, Lello ^a  

^a UNIVERSITY OF TUSCIA   (Italy)

^b UNIVERSITY OF VERONA   (Italy)

^c POLITECNICO DI MILANO   (Italy)

^d UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

Chlorophyll binding proteins; N formylkynurenine; Protein aggregation; Protein degradation; Reactive oxygen species; Thylakoid membranes

Indexed keywords

BINDING PROTEIN; CHLOROPHYLL A; CHLOROPHYLL B; CYTOCHROME B559; PEPTIDE; PROTEIN; PROTEIN PRECURSOR; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REACTIVE OXYGEN METABOLITE;

ARTICLE; CHLOROPLAST; ELECTRON SPIN RESONANCE; ELECTROSPRAY MASS SPECTROMETRY; ENZYME SUBUNIT; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ILLUMINATION; LIGHT HARVESTING SYSTEM; MAGNETIC FIELD; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PEPTIDE ANALYSIS; PHOTOSYNTHESIS; PHOTOSYSTEM I; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; SPINACH; THYLAKOID MEMBRANE; TWO DIMENSIONAL GEL ELECTROPHORESIS;

CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ELECTROPHORESIS; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; KYNURENINE; LIGHT; LIGHT-HARVESTING PROTEIN COMPLEXES; MAGNETICS; MASS SPECTROMETRY; MODELS, CHEMICAL; PEPTIDE MAPPING; PEPTIDES; PHOTIC STIMULATION; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; PROTEINS; PROTEOME; PROTEOMICS; REACTIVE OXYGEN SPECIES; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; THYLAKOIDS; TIME FACTORS;

SPINACIA OLERACEA;

EID: 29144481707     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr0502368     Document Type: Article

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