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FEBS Lett. 1993 Jul 12;326(1-3):246-50.

Immunopurification of a subcomplex of the NAD(P)H-plastoquinone-oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803.

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Institut für Entwicklungs- und Molekularbiologie der Pflanzen, Heinrich-Heine-Universität, Germany.

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  • FEBS Lett 1993 Sep 6;330(1):110.


An antibody against the NDH-K subunit of the NAD(P)H-dehydrogenase from the cyanobacterium Synechocystis sp. PCC6803 was used to isolate a subcomplex of the enzyme from Triton X-100 solubilized total membranes by immunoaffinity chromatography. The isolated subcomplex consisted of seven major polypeptides with molecular masses of 43, 27, 24, 21, 18, 14 and 7 kDa. The amino-terminal amino acid sequences of the polypeptides were determined. By comparing the sequences with the amino acid sequences deduced from DNA, three proteins were identified as NDH-H (43 kDa), NDH-K (27 kDa) and NDH-I (24 kDa). A fourth subunit (NDH-J, 21 kDa) was identified by Western blot analysis with an NDH-J antibody.

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