PMID: 6411579Jun 1, 1983Paper

The complete amino-acid sequence of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus

Hoppe-Seyler's Zeitschrift für physiologische Chemie
P FüglistallerH Zuber

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.

References

Nov 1, 1978·Hoppe-Seyler's Zeitschrift für physiologische Chemie·G FrankH Zuber
Jan 1, 1978·Annual Review of Biochemistry·P Y Chou, G D Fasman
Apr 1, 1976·Hoppe-Seyler's Zeitschrift für physiologische Chemie·G Frank, H Zuber

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Citations

Jan 1, 1986·Photosynthesis Research·B A Zilinskas, L S Greenwald
Aug 21, 1986·Journal of Immunological Methods·M N Kronick
Dec 1, 1994·Biophysical Chemistry·K F BradleyH L Crespi
Jan 1, 1986·Plant Physiology·D Guard-FriarR Maccoll
Oct 18, 2002·European Journal of Biochemistry·Georg WiegandWolfgang Reuter
Mar 2, 1999·Journal of Structural Biology·R MacColl
Nov 1, 1992·Photochemistry and Photobiology·W Rüdiger
Aug 9, 1990·Biochimica Et Biophysica Acta·R de LorimierS E Stevens
Mar 1, 1990·Journal of Bacteriology·L K Anderson, A R Grossman

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