Continuous monitoring of enzymatic activity within native electrophoresis gels: Application to mitochondrial oxidative phosphorylation complexes

Analytical Biochemistry

Volumn 431, Issue 1, 2012, Pages 30-39

  Covian, Raul ^a   Chess, David ^a   Balaban, Robert S ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

Blue native electrophoresis; In gel activity; Mitochondria; Oxidative phosphorylation

Indexed keywords

ASSOCIATION REACTIONS; CHROMOPHORES; ELECTROPHORESIS; GELS; KINETICS; LIGHT SCATTERING; MITOCHONDRIA; MONITORING; PHOSPHORYLATION; PROTEINS;

BLUE-NATIVE ELECTROPHORESIS; CONTINUOUS MONITORING; ENZYMATIC ACTIVITIES; GENERAL APPLICATIONS; MITOCHONDRIAL COMPLEX; MITOCHONDRIAL OXIDATIVE PHOSPHORYLATION; NATIVE GEL ELECTROPHORESIS; OXIDATIVE PHOSPHORYLATION;

REACTION KINETICS;

CYTOCHROME C; CYTOCHROME C OXIDASE; HEART MUSCLE EXTRACT; MITOCHONDRIAL PROTEIN;

ANIMAL TISSUE; ARTICLE; CORONARY ARTERY BLOOD FLOW; DIGITAL IMAGING; ENZYMATIC ASSAY; ENZYME ACTIVITY; ENZYME KINETICS; FLOW RATE; HEART MITOCHONDRION; IMAGE ANALYSIS; MITOCHONDRIAL RESPIRATION; MOLECULAR WEIGHT; NONHUMAN; OXIDATIVE PHOSPHORYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; REACTION TIME; SIGNAL NOISE RATIO; TURBIDITY;

EID: 84867113920     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2012.08.023     Document Type: Article

References (36)

1. H. Schagger, and G. von Jagow Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form Anal. Biochem. 199 1991 223 231
2. I. Wittig, H.P. Braun, and H. Schagger Blue native PAGE Nat. Protoc. 1 2006 418 428
3. H. Schagger, W.A. Cramer, and G. von Jagow Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis Anal. Biochem. 217 1994 220 230
4. H. Schagger, and K. Pfeiffer Supercomplexes in the respiratory chains of yeast and mammalian mitochondria EMBO J. 19 2000 1777 1783
5. R. Carrozzo, I. Wittig, F.M. Santorelli, E. Bertini, S. Hofmann, U. Brandt, and H. Schagger Subcomplexes of human ATP synthase mark mitochondrial biosynthesis disorders Ann. Neurol. 59 2006 265 275
6. I. Wittig, and H. Schagger Advantages and limitations of clear-native PAGE Proteomics 5 2005 4338 4346
7. I. Wittig, and H. Schagger Features and applications of blue-native and clear-native electrophoresis Proteomics 8 2008 3974 3990
8. I. Wittig, R. Carrozzo, F.M. Santorelli, and H. Schagger Functional assays in high-resolution clear native gels to quantify mitochondrial complexes in human biopsies and cell lines Electrophoresis 28 2007 3811 3820
9. I. Wittig, M. Karas, and H. Schagger High resolution clear native electrophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes Mol. Cell Proteomics 6 2007 1215 1225
10. K. Blinova, R.L. Levine, E.S. Boja, G.L. Griffiths, Z.D. Shi, B. Ruddy, and R.S. Balaban Mitochondrial NADH fluorescence is enhanced by complex I binding Biochemistry 47 2008 9636 9645
11. M. Saraste Oxidative phosphorylation at the fin de siecle Science 283 1999 1488 1493
12. D. Phillips, R. Covian, A.M. Aponte, B. Glancy, J.F. Taylor, D. Chess, and R.S. Balaban Regulation of oxidative phosphorylation complex activity: effects of tissue-specific metabolic stress within an allometric series and acute changes in workload Am. J. Physiol. Regul. Integr. Comp. Physiol. 302 2012 R1034 R1048
13. X. Grandier-Vazeille, and M. Guerin Separation by blue native and colorless native polyacrylamide gel electrophoresis of the oxidative phosphorylation complexes of yeast mitochondria solubilized by different detergents: specific staining of the different complexes Anal. Biochem. 242 1996 248 254
14. A.M. Seligman, M.J. Karnovsky, H.L. Wasserkrug, and J.S. Hanker Nondroplet ultrastructural demonstration of cytochrome oxidase activity with a polymerizing osmiophilic reagent, diaminobenzidine (DAB) J. Cell Biol. 38 1968 1 14
15. 2+-stimulated adenosine triphosphatase of Escherichia coli J. Bacteriol. 133 1978 287 292
16. E. Zerbetto, L. Vergani, and F. Dabbeni-Sala Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels Electrophoresis 18 1997 2059 2064
17. P.D. Boyer Catalytic site forms and controls in ATP synthase catalysis Biochim. Biophys. Acta 1458 2000 252 262
18. E. Bisetto, P.F. Di, M.P. Simula, I. Mavelli, and G. Lippe Mammalian ATPsynthase monomer versus dimer profiled by blue native PAGE and activity stain Electrophoresis 28 2007 3178 3185
19. S. Hong, and P.L. Pedersen ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas Microbiol. Mol. Biol. Rev. 72 2008 590 641
20. I. Wittig, B. Meyer, H. Heide, M. Steger, L. Bleier, Z. Wumaier, M. Karas, and H. Schagger Assembly and oligomerization of human ATP synthase lacking mitochondrial subunits A and A6L Biochim. Biophys. Acta 1797 2010 1004 1011
21. J.J. Garcia, E. Morales-Rios, P. Cortes-Hernandez, and J.S. Rodriguez-Zavala The inhibitor protein (IF1) promotes dimerization of the mitochondrial F1F0-ATP synthase Biochemistry 45 2006 12695 12703
22. V.K. Mootha, A.E. Arai, and R.S. Balaban Maximum oxidative phosphorylation capacity of the mammalian heart Am. J. Physiol. 272 1997 H769 H775
23. S.A. French, P.R. Territo, and R.S. Balaban Correction for inner filter effects in turbid samples: fluorescence assays of mitochondrial NADH Am. J. Physiol. 275 1998 C900 C909
24. 32P labeling of protein phosphorylation and metabolite association in the mitochondria matrix Methods Enzymol. 457 2009 63 80
25. F.W. Heineman, and R.S. Balaban Effects of afterload and heart rate on NAD(P)H redox state in the isolated rabbit heart Am. J. Physiol. 264 1993 H433 H440
26. R.S. Balaban, V.K. Mootha, and A. Arai Spectroscopic determination of cytochrome c oxidase content in tissues containing myoglobin or hemoglobin Anal. Biochem. 237 1996 274 278
27. Y. Li, M. D'Aurelio, J.H. Deng, J.S. Park, G. Manfredi, P. Hu, J. Lu, and Y. Bai An assembled complex IV maintains the stability and activity of complex I in mammalian mitochondria J. Biol. Chem. 282 2007 17557 17562
28. H. Schagger, and K. Pfeiffer The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes J. Biol. Chem. 276 2001 37861 37867
29. I.Y. Drobinskaya, I.A. Kozlov, M.B. Murataliev, and E.N. Vulfson Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1-ATPase, is located at the catalytic site of the enzyme FEBS Lett. 182 1985 419 424
30. 2+- and ADP-dependent inactivation during ATP hydrolysis Biochemistry 31 1992 12885 12892
31. Y.M. Milgrom, and P.D. Boyer The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic site Biochim. Biophys. Acta 1020 1990 43 48
32. +-ATP synthase from various species Biochem. Biophys. Res. Commun. 201 1994 487 492
33. P.D. Boyer The ATP synthase - a splendid molecular machine Annu. Rev. Biochem. 66 1997 717 749
34. D.M. Mueller, V. Indyk, and L. McGill ATPase kinetics for wild-type Saccharomyces cerevisiae F1-ATPase and F1-ATPase with the beta-subunit Thr197 → Ser mutation Eur. J. Biochem. 222 1994 991 999
35. S. Zhang, and A.T. Jagendorf Some unique characteristics of thylakoid unisite ATPase J. Biol. Chem. 270 1995 6607 6614
36. M.B. Murataliev, and P.D. Boyer The mechanism of stimulation of MgATPase activity of chloroplast F1-ATPase by non-catalytic adenine-nucleotide binding: acceleration of the ATP-dependent release of inhibitory ADP from a catalytic site Eur. J. Biochem. 209 1992 681 687