ライフサイエンスコーパス: submitochondrial particle

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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 ce of O2*- released from this preparation of submitochondrial particles.

5 t not the Q-free Ndi1, was incorporated into submitochondrial particles.

6 pyruvate suppressed superoxide production by submitochondrial particles, and attenuated oxidative str

7 indicate that complex I is inactivated when submitochondrial particles are treated with Ca2+.

8 t human factor B, which when added to bovine submitochondrial particles depleted of their factor B re

9 However, in submitochondrial particles devoid of antioxidant defense

10 with anti-OSCP IgG from a fraction of bovine submitochondrial particles enriched in oligomycin-sensit

11 NO. production obtained with homogenates and submitochondrial particles indicated that most of the en

12 hondrial NADH dehydrogenase (complex I) with submitochondrial particles isolated from Epstein-Barr vi

13 In bovine heart mitochondria and in submitochondrial particles, membrane-associated proteins

14 none markedly increased H2O2 production from submitochondrial particles oxidizing the complex I subst

15 In the study presented here, submitochondrial particles prepared from rat heart were

16 mitochondria, mitochondrial homogenates, and submitochondrial particles produced NO. (followed by the

17 Similarly, liver submitochondrial particles revealed a 44% decrease in th

18 When bovine heart submitochondrial particles (SMP) were illuminated with U

19 of Mrp1 in heart homogenate, sarcolemma, and submitochondrial particles (SMP) were increased 1.6-, 2-

20 c1 complex) has been studied in bovine heart submitochondrial particles (SMP) when cytochrome b was r

21 dox reaction of the bis-heme cytochrome b in submitochondrial particles (SMP), and all three inhibiti

22 tase (complex I) detected in tightly coupled submitochondrial particles (SMP).

23 nsfer pathway of complex III in bovine heart submitochondrial particles (SMP).

24 I, bc1 complex) were studied in bovine heart submitochondrial particles (SMP).

25 d that the rate of O-2 generation in cardiac submitochondrial particles (SMPs) was directly related t

26 The rate of (O2(./-)) generation by submitochondrial particles (SMPs) was inversely related

27 Furthermore, we had previously shown that in submitochondrial particles the affinity of complex I for

28 When Ndi1 was incorporated into bovine heart submitochondrial particles, the Q-bound form, but not th

29 Sprague-Dawley rat hearts and corresponding submitochondrial particles was studied.

30 Using submitochondrial particles, we confirmed that in the con

31 nalyses of rat liver mitochondria as well as submitochondrial particles were negative for any peptide

32 ure, never frozen rat liver mitochondria and submitochondrial particles were obtained.

33 Treatment of submitochondrial particles with protein kinase A and ATP

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