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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Electrophoresisarrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Electrophoresis
Article . 1998 . Peer-reviewed
License: Wiley Online Library User Agreement
Data sources: Crossref
Electrophoresis
Article . 1998
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Electrophoretic applications of phycobiliproteins

Authors: R, Aráoz; M, Lebert; D P, Häder;

Electrophoretic applications of phycobiliproteins

Abstract

AbstractPhycobiliproteins are homologous chromoproteins which constitute the phycobilisomes, the light harvesting complexes of the photosynthetic apparatus in cyanobacteria, rhodophyta and cryptophyta. In the present work, phycocyanin (PC) and Phycoerythrin (PE) from a Nostoc species are proposed as protein markers for electrophoretic techniques. Phycocyanin is a blue‐colored phycobiliprotein; it carries phycocyanobilin as chromophoric group and is composed of two subunits, α and β, with Mr of 14000 and 17000, respectively. In contrast, the PE subunits, having a similar Mr of 21000, are deep rose chromoproteins and carry phycoerythrobilin residues. Both low molecular weight phycobiliproteins are also suitable for monitoring protien blotting and the focusing time of protein samples during isoelectric focusing as internal markers. The PE subunits which form a single broad band after sodium dodecyl sulfate‐polyacrylamide gel electrophoresis have different isoelectric points, and they form two visible bands when they reach their isoelectric point. The phycobilisomes constitute up to 50% of the total protein in cyanobacteria and their content in PC or PE can be up‐ or down‐regulated by using different light conditions (chromatic adaptation).

Related Organizations
Keywords

Bacterial Proteins, Light-Harvesting Protein Complexes, Phycobilisomes, Phycocyanin, Electrophoresis, Polyacrylamide Gel, Phycoerythrin, Isoelectric Focusing, Cyanobacteria, Plant Proteins

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
31
Top 10%
Top 10%
Top 10%
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