Immunopurification of a subcomplex of the NAD(P)H-plastoquinone-oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803.
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.
Berger
S
S
Institut für Entwicklungs- und Molekularbiologie der Pflanzen, Heinrich-Heine-Universität, Germany.
Ellersiek
U
U
Kinzelt
D
D
Steinmüller
K
K
D000595:Amino Acid Sequence; D015153:Blotting, Western; D002846:Chromatography, Affinity; D000458:Cyanobacteria / Q000201:enzymology*; D015151:Immunoblotting; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification*
D009247:NADH, NADPH Oxidoreductases; C072396:NAD(P)H plastoquinone oxidoreductase