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LHC II-Apoproteins of Chlamydomonas Reinhardii: Isolation, Isoelectric Focusing, Association with Lipids

  • M. Sigrist
  • C. Zwillenberg-Fridman
  • Ch. Giroud
  • W. Eichenberger
  • A. Boschetti
Part of the NATO ASI Series book series (NSSA, volume 168)

Abstract

Light-harvesting chlorophyll a/b-protein complexes of the photosystem II (LHC II) are major components of thylakoids, and they contain chlorophyll a and b, xantophylls and 2–5 hydrophobic proteins, the LHC II-apoproteins.1 In the green alga Chlamydomonas reinhardii, there exist three immunologically cross-reacting LHC II-apoproteins of 24, 25 and 29 kD.2 Up to now, only phosphorylation and the blocked N-terminus are known as secondary modifications. We developed a method for the isolation of the LHC II-apoproteins on a preparative scale and characterized them by isoelectric focusing (IEF) and analysis of secondary modifications, such as binding of lipids or fatty acids. Furthermore, the apoproteins of a chlorophyll b-defi-cient mutant (pg 113), 2 from which the LHC II-complex can not be isolated, have been studied.

Keywords

Palmitic Acid Parent Strain Fatty Acid Analysis Preparative Scale Secondary Modification 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • M. Sigrist
    • 1
  • C. Zwillenberg-Fridman
    • 1
  • Ch. Giroud
    • 1
  • W. Eichenberger
    • 1
  • A. Boschetti
    • 1
  1. 1.Institut für BiochemieUniversität BernBernSwitzerland

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