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BY-NC-ND 3.0 license Open Access Published by De Gruyter June 2, 2014

Reconstitution of an Allophycocyanin Trimer Complex Containing the C-Terminal 21-23 kDa Domain of the Core-Membrane Linker Polypeptide Lcm

Lothar Gottschalk, Friedrich Lottspeich and Hugo Scheer

Abstract

Allophycocyanin (AP) was isolated from extracts of the cyanobacterium Mastigocladus laminosus. A fraction enriched in AP-associated polypeptides with apparent molecular masses of 21 -23 kD a in SDS-PAGE, was isolated on a preparative scale and identified as a homolo­gous mixture of C-terminal fragments of the core-membrane linker polypeptide Lcm. The complex (αAPβAP)3 ·21 -23 kD a was reconstituted and characterized by sucrose density gradient ultracentrifugation, absorption, fluorescence emission and circular dichroism spectroscopy. The 21 -23 kD a polypeptides were found to induce spectral changes in AP similar to those induced by the small core linker polypeptide Lc8.9. Possible functions of the complex in phycobilisomes are discussed.

Received: 1994-2-18
Published Online: 2014-6-2
Published in Print: 1994-6-1

© 1946 – 2014: Verlag der Zeitschrift für Naturforschung

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

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