The Complete Amino Acid Sequence of Both Subunits of Allophycocyanin, a Light Harvesting Protein-Pigment Complex from the CyanobacteriumMastigocladus laminosus
- 1 January 1981
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 362 (1), 611-628
- https://doi.org/10.1515/bchm2.1981.362.1.611
Abstract
The amino acid sequences of the .alpha.- and .beta.-subunit of allophycocyanin, a water-soluble [photosynthetic] light-harvesting protein-pigment complex from the thermophilic cyanobacterium M. laminosus, was determined. The .alpha.-chain consists of 160 amino acid residues and the .beta.-chain of 161 amino acid residues. The homology of the .alpha.- and .beta.-chains is 37%. A comparison with C-phycocyanin reveals that the 2nd chromophore of the C-phycocyanin .beta.-subunit is attached to an inserted peptide of 10 amino acid residues at position 151-160.This publication has 14 references indexed in Scilit:
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