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Allo phycocyanin b a common beta subunit in synechococcus allo phycocyanin b maximum wavelength 670 nanometers and allo phycocyanin maximum wavelength 650 nanometers

Allo phycocyanin b a common beta subunit in synechococcus allo phycocyanin b maximum wavelength 670 nanometers and allo phycocyanin maximum wavelength 650 nanometers

Journal of Biological Chemistry 256(23): 12600-12606

In cyanobacterial phycobilisomes, light energy absorbed by phycocyanin (.lambda.max 620 nm) is transferred to allophycocyanin (AP; .lambda.max 650 nm) and allophycocyanin B (AP-B; .lambda.max 670 nm) and emitted primarily at 680 nm. This emission maximum coincides with that of prue AP-B. Synechococcus 6301 AP and AP-B are (.alpha.beta.)3 trimers with a number of similar properties. The .beta. subunits of AP and AP-B have identical MW, isoelectric points, absorption spectra, NH2-terminal sequences, yield almost indistinguishable tryptic peptide maps and can substitute for each other in hybridization with the .alpha. subunits. Apparently, the .beta. subunits are identical polypeptides. By the same criteria, the .alpha. subunits of these 2 proteins are clearly unique polypeptides. The .alpha. subunits carry the information which determines the absorption and fluorescence emission spectra of the proteins. The hybrid of the .alpha. subunits of AP-B with the .beta. subunits of AP has a .lambda.max of 670 nm and an emissionmaximum of 680 nm. In mixtures of AP-B and AP, heterologous trimers are formed in a near-statistical manner by subunit exchange. In such trimers, AP-B .alpha.beta. monomers act as terminal energy acceptors.

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Accession: 004698844

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