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1 es of experiments with both mitochondria and submitochondrial particles.
2 ygen consumption of cells, mitochondria, and submitochondrial particles.
3 g helices 2 and 3 of QPs3, in mitoplasts and submitochondrial particles.
4 nthetic activities of ATP synthase in bovine submitochondrial particles.
5 ce of O2*- released from this preparation of submitochondrial particles.
6 t not the Q-free Ndi1, was incorporated into submitochondrial particles.
7 pyruvate suppressed superoxide production by submitochondrial particles, and attenuated oxidative str
9 t human factor B, which when added to bovine submitochondrial particles depleted of their factor B re
11 with anti-OSCP IgG from a fraction of bovine submitochondrial particles enriched in oligomycin-sensit
12 NO. production obtained with homogenates and submitochondrial particles indicated that most of the en
13 hondrial NADH dehydrogenase (complex I) with submitochondrial particles isolated from Epstein-Barr vi
15 none markedly increased H2O2 production from submitochondrial particles oxidizing the complex I subst
17 mitochondria, mitochondrial homogenates, and submitochondrial particles produced NO. (followed by the
20 of Mrp1 in heart homogenate, sarcolemma, and submitochondrial particles (SMP) were increased 1.6-, 2-
21 c1 complex) has been studied in bovine heart submitochondrial particles (SMP) when cytochrome b was r
22 dox reaction of the bis-heme cytochrome b in submitochondrial particles (SMP), and all three inhibiti
26 d that the rate of O-2 generation in cardiac submitochondrial particles (SMPs) was directly related t
28 Furthermore, we had previously shown that in submitochondrial particles the affinity of complex I for
29 When Ndi1 was incorporated into bovine heart submitochondrial particles, the Q-bound form, but not th
32 nalyses of rat liver mitochondria as well as submitochondrial particles were negative for any peptide