LHC II-Apoproteins of Chlamydomonas Reinhardii: Isolation, Isoelectric Focusing, Association with Lipids
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.
KeywordsPalmitic Acid Parent Strain Fatty Acid Analysis Preparative Scale Secondary Modification
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