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Structural relationships between the NADH dehydrogenases of Paracoccus denitrificans and bovine heart mitochondria as revealed by immunological cross‐reactivities
Author(s) -
George Christina L.,
Ferguson Stuart J.,
Cleeter Michael W.J.,
lan Ragan C.
Publication year - 1986
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(86)81199-1
Subject(s) - paracoccus denitrificans , nadh dehydrogenase , biochemistry , protein subunit , dehydrogenase , mitochondrion , enzyme , biology , succinate dehydrogenase , microbiology and biotechnology , chemistry , gene
An antibody raised against two subunits ( M r , 48000 and 25000) of NADH dehydrogenase from Paracoccus denitrificans cross‐reacts with one of more than 20 polypeptides that form the bovine heart mitochondrial NADH dehydrogenase. The cross‐reacting subunit has M r , 51000 and is believed to be the NADH‐binding subunit of the enzyme. Antibodies raised against certain subunits of the bovine heart NADH dehydrogenase were tested for cross‐reactivity with P . denitrificans cytoplasmic membranes. Of those tested, only one, an antibody specific for the 49 kDa subunit of mitochondrial NADH dehydrogenase, cross‐reacted with the bacterial membranes. It recognised a polypeptide of approximate M r , 46000. This is an indication for a previously undetected third subunit of NADH dehydrogenase from P . denitrificans . The immunological crossreactions indicate that the NADH dehydrogenases from P . denitrificans and bovine heart mitochondria are related structurally.