The Complete Amino-Acid Sequence of Both Subunits of Phycoerythrocyanin from the Thermophilic CyanobacteriumMastigocladus laminosus
- 1 January 1983
- journal article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (1), 691-712
- https://doi.org/10.1515/bchm2.1983.364.1.691
Abstract
The amino-acid sequences of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus have been determined. The alpha-subunit consists of 162 amino-acid residues and has a molecular mass of 18200 Da. The beta-subunit is 171 residues long and has a molecular mass of 19600 Da. The tetrapyrrole chromophores are bound at position 84 in the alpha- and beta-subunits and at position 155 in the beta-subunit. The homology between the two subunits is 21%. The homologies between the phycoerythrocyanin subunits and the corresponding subunits of C-phycocyanin and allophycocyanin are 63% and 26% for the alpha-subunits and 67% and 36% for the beta-subunits, respectively. Secondary structure predictions were calculated for all six subunits of the phycobiliproteins from M. laminosus. The most conservative regions of the biliproteins were found in segments C-terminal to the chromophore-binding sites.Keywords
This publication has 13 references indexed in Scilit:
- Primary structure of phycocyanin from the unicellular rhodophyte Cyanidium caldarium. I. Complete amino acid sequence of the alpha subunit.Journal of Biological Chemistry, 1981
- Primary structure of phycocyanin from the unicellular rhodophyte Cyanidium caldarium. II. Complete amino acid sequence of the beta subunit.Journal of Biological Chemistry, 1981
- The Complete Amino Acid Sequence of Both Subunits of Allophycocyanin, a Light Harvesting Protein-Pigment Complex from the CyanobacteriumMastigocladus laminosusHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1981
- SHORT COMMUNICATIONHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
- Empirical Predictions of Protein ConformationAnnual Review of Biochemistry, 1978
- Picosecond time-resolved energy transfer in Porphyridium cruentum. Part I. In the intact algaBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1978
- Structural studies on phycobiliproteins II. C-phycocyanin: amino acid sequence of the beta subunit. Specific cleavage of the alpha subunit.Journal of Biological Chemistry, 1978
- The Complete Amino Acid Sequence of Both Subunits of C-Phycocyanin from the CyanobacteriumMastigocladus laminosusHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1978
- The Complete Amino Acid Sequences of Both Subunits of the Sweet Protein MonellinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- On the Hydrazinolysis of Proteins and Peptides: A Method for the Characterization of Carboxyl-terminal Amino Acids in ProteinsBulletin of the Chemical Society of Japan, 1952