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Isolation and characterization of phycoerythrocyanin and chromatic adaptation of the thermophilic cyanobacteriumMastigocladus laminosus

✍ Scribed by Paul Füglistaller; Herbert Widmer; Walter Sidler; Gerhard Frank; Herbert Zuber

Book ID
104764878
Publisher
Springer
Year
1981
Tongue
English
Weight
885 KB
Volume
129
Category
Article
ISSN
0302-8933

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✦ Synopsis

The thermophili c cyanobacterium Mastigocladus larninosus exhibits chromatic adaptation: In green light the production of the phycobiliprotein phycoerythrocyanin is enhanced drastically.

Phycoerythrocyanin was characterised with respect to its molecular weight, isoelectric point, absorption spectra and size of its aggregates. The two subunits of the protein were separated and characterised according to these criteria. Their chromophore contents, amino acid compositions and Nterminal amino acid sequences were also determined. The sequences were compared with those of allophycocyanin and C-phycocyanin from MastigocIadus laminosus.

📜 SIMILAR VOLUMES

Biliprotein assembly in the hemidiscoida
Biliprotein assembly in the hemidiscoidal phycobilisomes of the thermophilic cyanobacteriumMastigocladus laminosusCohn. Characterization of dissociation products with special reference to the peripheral phycoerythrocyanin-phycocyanin complexes
✍ Michael Nies; Werner Wehrmeyer 📂 Article 📅 1981 🏛 Springer 🌐 English ⚖ 855 KB

The dissociation products of isolated phycobilisomes of Mastigocladus laminosus were separated and analyzed by ultracentrifugation and, in part, by isoelectric focusing. With the exception of the allophycocyanin core, the sedimentation constants of peripheral phycocyanin-and phycoerythrocyanin-phyco