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rdf:type |
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lifeskim:mentions |
umls-concept:C0002028,
umls-concept:C0020792,
umls-concept:C0023693,
umls-concept:C0031916,
umls-concept:C0033684,
umls-concept:C0052221,
umls-concept:C0220781,
umls-concept:C0330390,
umls-concept:C0332157,
umls-concept:C0679209,
umls-concept:C0996246,
umls-concept:C1260956,
umls-concept:C1555707,
umls-concept:C1705851,
umls-concept:C1711351,
umls-concept:C1749467,
umls-concept:C1998793,
umls-concept:C2003941,
umls-concept:C2752151,
umls-concept:C2828366
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pubmed:issue |
1
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pubmed:dateCreated |
1997-2-21
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pubmed:abstractText |
Much controversy exists as to the level at which light exerts control over the biosynthesis of the photosynthetic apparatus in higher plants and other organisms. The eukaryotic red alga Cyanidium caldarium, like higher plants, undergoes light induction of chlorophyll synthesis. In addition to chlorophyll a the alga also synthesises the linear tetrapyrrole phycocyanobilin, which is combined with alpha or beta apobiliproteins to form phycocyanin, the major light-harvesting pigment in this organism. We have previously shown that the tetrapyrrole precursor 5-aminolaevulinic acid (ALA) can substitute for light in inducing the biosynthesis of the phycocyanobilin moiety of this protein. We have also described the appearance of a protein of similar isoelectric point and molecular weight to phycocyanin in ALA-fed cells (Turner et al., 1992, Plant Physiol Biochem 30: 309-314). We now report on the protein's immunological and sequence identity with phycocyanin alpha and beta subunits, and provide further evidence that bilin-apoprotein ligation is light dependent.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
B
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0032-0935
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
201
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
78-83
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9004549-Amino Acid Sequence,
pubmed-meshheading:9004549-Aminolevulinic Acid,
pubmed-meshheading:9004549-Animals,
pubmed-meshheading:9004549-Blotting, Western,
pubmed-meshheading:9004549-Chromatography, Gel,
pubmed-meshheading:9004549-Culture Media,
pubmed-meshheading:9004549-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9004549-Isoelectric Focusing,
pubmed-meshheading:9004549-Light,
pubmed-meshheading:9004549-Male,
pubmed-meshheading:9004549-Molecular Sequence Data,
pubmed-meshheading:9004549-Photosynthesis,
pubmed-meshheading:9004549-Phycocyanin,
pubmed-meshheading:9004549-Pigments, Biological,
pubmed-meshheading:9004549-Plant Proteins,
pubmed-meshheading:9004549-Rabbits,
pubmed-meshheading:9004549-Rhodophyta,
pubmed-meshheading:9004549-Sodium Dodecyl Sulfate,
pubmed-meshheading:9004549-Solutions
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pubmed:year |
1997
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pubmed:articleTitle |
Purification and identification of apophycocyanin alpha and beta subunits from soluble protein extracts of the red alga Cyanidium caldarium. Light exposure is not a prerequisite for biosynthesis of the protein moiety of this photosynthetic accessory pigment.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Leeds, UK. bmblt@leeds.ac.uk
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pubmed:publicationType |
Journal Article
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