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Bili protein assembly in the disc shaped phycobilisomes of rhodella violacea electron microscopic and biochemical analyses of c phycocyanin and allo phycocyanin aggregates



Bili protein assembly in the disc shaped phycobilisomes of rhodella violacea electron microscopic and biochemical analyses of c phycocyanin and allo phycocyanin aggregates



Archives of Microbiology 125(1-2): 43-52



C-phycocyanin and allophycocyanin from the red alga R. violacea were investigated by EM and biochemical methods using samples taken from the same fractions. The MW of the native biliprotein aggregates C-phycocyanin and allophycocyanin are about 139,000 (140,000) and 130,000 (145,000) as revealed by calibrated gel chromatography, gradient gel electrophoresis and morphological measurements on the basis of an average protein packing density. These MW are direct evidence for a trimeric aggregation from (.alpha.beta.)3 of these biliproteins. Independently, their monomers were determined to be about 34,400 (C-phycocyanin) and 33,900 (allophycocyanin). C-phycocyanin and allophycocyanin are ring-shaped, 6-membered, biliprotein aggregates with dimensions of about 10.2 .times. 3.0 nm and 10.0 .times. 3.0 nm, respectively. The aggregates are made up of 6 subunits, 3.alpha. and 3.beta., which are assumed to be associated in alternating positions. They are arranged in regular hexagons in C6 symmetry. Hexameric aggregates (.alpha.beta.)6, so far only isolated for C-phycocyanin, originate by face to face association of 2 trimeric aggregates.

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Accession: 004824551

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DOI: 10.1007/bf00403196



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