Immunological assays of the NADH dehydrogenase content of bovine heart mitochondria and submitochondrial particles

FEBS Letters ◽  
1980 ◽  
Vol 110 (2) ◽  
pp. 279-282 ◽  
Author(s):  
Stuart Smith ◽  
Ian R. Cottingham ◽  
C.Ian Ragan
Keyword(s):  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Immunological Assays

scholarly journals Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria

1980 ◽  
Vol 191 (2) ◽  
pp. 421-427 ◽  
Author(s):  
J F Turrens ◽  
A Boveris
Keyword(s):  
Cytochrome B ◽  
Nadh Dehydrogenase ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Biphasic Effect ◽  
Carbonyl Cyanide ◽  
Autocatalytic Process ◽  
Ph Range ◽  
Energy Dependent ◽  
O2 Production

Submitochondrial particles from bovine heart in which NADH dehydrogenase is reduced by either addition of NADH and rotenone or by reversed electron transfer generate 0.9 +/- 0.1 nmol of O2-/min per mg of protein at pH 7.4 and at 30 degrees C. When NADH is used as substrate, rotenone, antimycin and cyanide increase O2- production. In NADH- and antimycin-supplemented submitochondrial particles, rotenone has a biphasic effect: it increases O2- production at the NADH dehydrogenase and it inhibits O2- production at the ubiquinone-cytochrome b site. The generation of O2- by the rotenone, the uncoupler carbonyl cyanide rho-trifluoromethoxyphenylhydrazone and oligomycin at concentrations similar to those required to inhibit energy-dependent succinate-NAD reductase. Cyanide did not affect O2- generation at the NADH dehydrogenase, but inhibited O2- production at the ubiquinone-cytochrome b site. Production of O2- at the NADH dehydrogenase is about 50% of the O2- generation but the ubiquinone-cytochrome b area at pH 7.4. Additivity of the two mitochondrial sites of O2- generation was observed over the pH range from 7.0 to 8.8. AN O2–dependent autocatalytic process that requires NADH, submitochondrial particles and adrenaline is described.

scholarly journals A simple and rapid method for the preparation of adenosine triphosphatase from submitochondrial particles

1975 ◽  
Vol 148 (3) ◽  
pp. 533-537 ◽  
Author(s):  
R B Beechey ◽  
S A Hubbard ◽  
P E Linnett ◽  
A D Mitchell ◽  
E A Munn
Keyword(s):  
Electron Microscopy ◽  
Rapid Method ◽  
Adenosine Triphosphatase ◽  
Pure Form ◽  
Heart Mitochondria ◽  
Polyacrylamide Gels ◽  
Submitochondrial Particles ◽  
Bovine Heart

An almost pure form of the bovine heart mitochondrial adenosine triphosphatase (ATPase) is released from the membrane by shaking submitochondrial particles with chloroform. Analyses on polyacrylamide gels and by electron microscopy, and also sensitivity to inhibitors, show that the chloroform-released enzyme is similar to other ATPase preparations from bovine heart mitochondria.

scholarly journals The Primary Structure of Subunit II of NADH Dehydrogenase from Bovine-Heart Mitochondria

1983 ◽  
Vol 134 (1) ◽  
pp. 145-150 ◽  
Author(s):  
Hedvig BAHR-LINDSTROM ◽  
Yves M. GALANTE ◽  
Magnus PERSSON ◽  
Hans JORNVALL
Keyword(s):  
Primary Structure ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
Bovine Heart

scholarly journals The polypeptide composition of the mitochondrial NADH: ubiquinone reductase complex from several mammalian species

1985 ◽  
Vol 230 (3) ◽  
pp. 739-746 ◽  
Author(s):  
M W Cleeter ◽  
C I Ragan
Keyword(s):  
Nadh Dehydrogenase ◽  
Mammalian Species ◽  
Polypeptide Composition ◽  
Submitochondrial Particles ◽  
Protein Subunits ◽  
Bovine Heart ◽  
Nadh:Ubiquinone Reductase ◽  
Monospecific Antisera

The polypeptide composition of isolated mitochondrial NADH:ubiquinone reductase (NADH dehydrogenase) is very similar to that of material immunoprecipitated from detergent-solubilized bovine heart submitochondrial particles by antisera to the holoenzyme. The specificity of the antisera for dehydrogenase polypeptides was determined by immunoblotting, which showed that antisera reacting with only a few proteins were able to immunoprecipitate all others in parallel. The polypeptide compositions of rat, rabbit and human NADH dehydrogenase were determined by immunoprecipitation of the enzyme from solubilized submitochondrial particles and proved to be very similar to that of the bovine heart enzyme, particularly in the high-Mr region. Further homologies in these and other species were explored by immunoblotting with antisera to the holoenzyme and monospecific antisera raised against iron-sulphur-protein subunits of the enzyme.

Kinetic of Superoxide Formation by Respiratory Chain NADH-Dehydrogenase of Bovine Heart Mitochondria

1983 ◽  
Vol 94 (4) ◽  
pp. 1301-1306 ◽  
Author(s):  
Dongchon KANG ◽  
Hideki NARABAYASHI ◽  
Takeyoshi SATA ◽  
koichiro TAKESHIGE
Keyword(s):  
Respiratory Chain ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
Bovine Heart ◽  
Superoxide Formation

scholarly journals THE PRIMARY STRUCTURE OF SUBUNIT II OF NADH DEHYDROGENASE FROM BOVINE-HEART MITOCHONDRIA

1983 ◽  
Vol 134 (1) ◽  
pp. 149-150
Author(s):  
Hedvig Bahr-Lindstrom ◽  
Yves M. Galante ◽  
Magnus Persson ◽  
Hans Jornvall
Keyword(s):  
Primary Structure ◽  
Nadh Dehydrogenase ◽  
Heart Mitochondria ◽  
Bovine Heart
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