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Immunopurification of a subcomplex of the NAD(P)H‐plastoquinone‐oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803
Author(s) -
Berger Susanne,
Ellersiek Ulrike,
Kinzelt Dagmar,
Steinmüller Klaus
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81800-f
Subject(s) - synechocystis , protein subunit , oxidoreductase , biochemistry , nad+ kinase , biology , amino acid , western blot , microbiology and biotechnology , peptide sequence , nadh dehydrogenase , plastoquinone , enzyme , thylakoid , chloroplast , gene , mutant
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.