The major peptidyl-prolyl isomerase activity in thylakoid lumen of plant chloroplasts belongs to a novel cyclophilin TLP20

FEBS Letters

Volumn 542, Issue 1-3, 2003, Pages 137-141

  Edvardsson, Anna ^a   Eshaghi, Said ^a,b   Vener, Alexander V ^a   Andersson, Bertil ^a,b  

^a LINKÖPING UNIVERSITY   (Sweden)

^b STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

Cyclophilin; Mass spectrometry; Peptidyl prolyl isomerase activity; Spinach; Thylakoid lumen

Indexed keywords

AMINO ACID; CYCLOPHILIN; CYCLOSPORIN A; THYLAKOID LUMEN PEPTIDYLPROLYL ISOMERASE OF 20 KDA; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARABIDOPSIS; ARTICLE; CATALYST; CHLOROPLAST; CHROMOSOME 5; CLASSIFICATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME INHIBITION; GENE INSERTION; GENETIC CODE; MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; RICE; SPINACH; THYLAKOID;

ARABIDOPSIS; NUCLEOPOLYHEDROVIRUS; SPINACIA OLERACEA;

EID: 0037728922     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(03)00366-1     Document Type: Article

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