The Phycobiliprotein β16.2of the Allophycocyanin Core from the CyanobacteriumMastigodadus laminosus.Characterization and Complete Amino-Acid Sequence
- 1 January 1987
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 368 (1) , 1-10
- https://doi.org/10.1515/bchm3.1987.368.1.1
Abstract
The minor phycobiliprotein .beta.16.2 was isolated from the APC-core of phycobilisomes from the cyanobacterium Mastigocladus laminosus. Its complete amino-acid sequence and some spectral characteristics are presented. .beta.16.2 consists of 169 amino acids and its molecular mass is 19390 Da. A phycocyanobilin chromophore is covalently bound to a cysteine at position 84 as in all other phycobiliproteins. The first 138 amino acids are highly homologous to the N-terminal part of .beta.AP (62.5%), whereas the C-terminal part has no homology. The absorption maximum is situated at 624 nm, the fluorescence emission maximum at 644 nm in phosphate buffer, pH 7.0. Both values are slightly redshifted compared with .alpha.AP and .beta.AP.This publication has 8 references indexed in Scilit:
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