ArticlePlanta1997
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.
Article in Planta, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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0 citing papers in PubMed, 5 citations in OpenAlex.
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3 authors at 1 institution in 1 country.
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Abstract
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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