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Isolation and Biliprotein Characterization of Phycobilisomes from the Thermophilic Cyanobacterium Mastigocladus laminosus Cohn

Michael Nies and Werner Wehrmeyer
Planta
Vol. 150, No. 4 (1980), pp. 330-337
Published by: Springer
Stable URL: http://www.jstor.org/stable/23374970
Page Count: 8
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Isolation and Biliprotein Characterization of Phycobilisomes from the Thermophilic Cyanobacterium Mastigocladus laminosus Cohn
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Abstract

A method for the effective isolation of functionally intact phycobilisomes from the thermophilic cyanobacterium M. laminosus is presented, using an unconventional high buffer molarity for stabilizing the aggregates and introducing a DNAse treatment of the disrupted cells to obtain sharp banding of the phycobilisomes in the linear sucrose density gradients. The structural integrity of the isolated phycobilisomes is demonstrated by a fluorescence emission maximum at 673 nm of aggregated allophycocyanin and by electron microscopy. Besides C-phycocyanin and allophycocyanin, phycoerythrocyanin is a constituent pigment of the phycobilisomes. These pigments, indicated in the absorption spectrum of phycobilisomes with a maximum at 610 nm and two shoulders at 650 and 580 nm, respectively, were characterized by spectral data and isoelectric points.

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