Abstract
Reconstitution of biological systems has proven a most valuable tool for the elucidation of multicomponent biochemical pathways. The study of a biological activity in both partially resolved or highly purified systems necessitates the assay of a specific, well-defined functional property of an enzyme or protein complex. In contrast to studies of soluble enzymatic complexes in homogeneous solution wherein the reactants and products may be readily distinguished from each other, the biological activity of a number of membrane processes is the translocation of a species from one compartment to another via passive, coupled, or active transport mechanisms. The biological activity may also be dependent upon a receptor-ligand interaction resulting in the change in a membrane permeability or the activation of an enzymatic complex. Each of these different functions, namely passive transport systems, receptor or voltage-dependent permeabilities, coupled transport, and the energy-transducing ATPases, is amenable to studies in reconstituted membranes.
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References
Racker, E., B. Violand, S. O’Neal, M. Alfonzo, and J. Telford. 1979. Reconstitution, a way of biochemical research; some new approaches to membrane-bound enzymes. Arch. Biochem. Biophys. 198: 470–477.
Hokin, L. E. 1981. Reconstitution of “carriers” in artificial membranes. J. Membr. Biol. 60: 77–93.
Miller, C., and E. Racker. 1979. Reconstitution of membrane transport functions. In: The Receptors. R. D. O’Brien, ed. Plenum Press, New York. pp. 1–31.
Loomis, W. F., and F. Lippmann. 1948. Reversible inhibition of the coupling between phosphorylation and oxidation. J. Biol. Chem. 172: 807–808.
Hopfer, U., A. L. Lehninger, andT. E. Thompson. 1968. Protonic conductance across phospholipid bilayer membranes induced by uncoupling agents for oxidative phosphorylation. Proc. Natl. Acad. Sci. USA 59: 489–490.
Lardy, H. A., D. Johnson, and W. C. McMurray. 1958. Antibiotics as tools for metabolic studies. I. A survey of toxic antibiotics in respiratory, phosphorylation and glycolytic systems. Arch. Biochem. Biophys. 78: 587–597.
Boyer, P. D., A. B. Falcone, and W. H. Harrison. 1954. Reversal and mechanism of oxidative phosphorylation. Nature (London) 174: 401–402.
Penefsky, H. S., M. E. Pullman, A. Datta, and E. Racker. 1960. Partial resolution of the enzymes catalyzing oxidative phosphorylation. II. Participation of a soluble adenosine triphosphatase in oxidative phosphorylation. J. Biol. Chem. 235: 3330–3336.
Cooper, C., and A. L. Lehninger. 1957. Oxidative phosphorylation by an enzyme complex from extracts of mitochondria. V. The adenosine triphosphate-phosphate exchange reaction. J. Biol. Chem. 224: 561–578.
Horstman, L., and E. Racker. 1970. Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXII. Interaction between mitochondrial adenosine triphosphatase inhibitor and mitochondrial adenosine triphosphatase. J. Biol. Chem. 245: 1336–1344.
Racker, E. 1963. A mitochondrial factor conferring oligomycin sensitivity on soluble mitochondrial ATPase. Biochem. Biophys. Res. Commun. 10: 435–439.
Racker, E. 1962. Studies on factors involved in oxidative phosphorylation. Proc. Natl. Acad. Sci. USA 48: 1659–1663.
Racker, E., and T. E. Conover. 1963. Multiple coupling factors in oxidative phosphorylation. Fed. Proc. 22: 1088–1091.
Kagawa, Y., and E. Racker. 1966. Partial resolution of the enzymes catalyzing oxidative phosphorylation. XIII. Properties of a factor conferring oligomycin sensitivity on mitochondrial adenosine triphosphatase. J. Biol. Chem. 241: 2461–2466.
Arion, W. J., and E. Racker. 1970. Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXIII. Preservation of energy coupling in submitochondrial particles lacking cytochrome oxidase. J. Biol. Chem. 245: 5186–5194.
Kagawa, Y., and E. Racker. 1966. Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXV. Reconstitution of vesicles catalyzing 32P-adenosine triphosphate exchange. J. Biol. Chem. 241: 5477–5487.
Mitchell, P. 1966. Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol. Rev. 41: 445–502.
Racker, E. 1972. Reconstitution of cytochrome oxidase vesicles and conferral of sensitivity to energy transfer inhibitors. J. Membr. Biol. 10: 221–235.
Racker, E., and A. Kandrach. 1973. Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXIX. Reconstitution of the third segment of oxidative phosphorylation. J. Biol. Chem. 248: 5841–5847.
Ragan, G. F., and E. Racker. 1973. Partial resolution of the en-zymes catalyzing oxidative phosphorylation. XXVIII. The reconstitution of the first site of energy conservation. J. Biol. Chem. 248: 2563–2569.
Boyer, P. D. 1964. Carboxyl activation as a possible common reaction in substrate-level and oxidative phosphorylation and in muscle contraction. In: Oxidases and Related Redox Systems. T. E. King, H. S. Muson, and M. Morrison, eds. Wiley, New York. pp. 994–1017.
Racker, E., and W. Stoeckenius. 1974. Reconstitution of purple membrane vesicles catalyzing light driven proton uptake and adenosine triphosphate formation. J. Biol. Chem. 249: 662–663.
Kagawa, Y., K. Ohno, M. Yoshida, Y. Takeuchi, and N. Sone. 1977. Proton translocation by ATPase and bacteriorhodopsin. Fed. Proc. 36: 1815–1818.
Winget, G. D., N. Kanner, and E. Racker. 1977. Formation of ATP by the adenosine triphosphatase complex from spinach chloroplasts reconstituted together with bacteriorhodopsin. Biochim. Biophys. Acta 460: 490–499.
Poyton, R. V., and G. Schatz. 1975. Cytochrome c oxidase from baker’s yeast. III. Physical characterization of isolated subunits and chemical evidence for two different classes of polypeptides. J. Biol. Chem. 250: 752–761.
Werner, S. 1977. Preparation of polypeptide subunits of cytochrome oxidase from Neurospora crassa. Eur. J. Biochem. 79: 103–110.
Carroll, R. C., and E. Racker, 1977. Preparation and characterization of cytochrome c oxidase vesicles with high respiratory control. Biol. Chem. 252: 6981–6990.
Malmstrom, B. G. 1979. Cychrome c oxidase structure and catalytic activity. Biochim. Biophys. Acta 549: 281–303.
Hinkle, P. C., J. J. Kim, and E. Racker. 1972. Ion transport and respiratory control in vesicles formed from cytochrome oxidase and phospholipids. J. Biol. Chem. 247: 1338–1339.
Hinkle, P. C. 1973. Electron transfer across membranes and energy coupling. Fed. Proc. 32: 1988–1992.
Racker, E. 1972. Reconstitution of cytochrome oxidase vesicles and conferral of sensitivity to energy transfer inhibitors. J. Membr. Biol. 10: 221–235.
Racker, E., and A. Kandrach. 1973. Partial resolution of the enzyme catalyzing oxidative phosphorylation. XXIX. Reconstitution of the third segment of oxidative phosphorylation. J. Biol. Chem. 248: 5841–5847.
Wikstrom, M. K. F., and H. T. Suari. 1977. The mechanism of energy conservation and transduction by mitochondrial cytochrome c oxidase. Biochim. Biophys. Acta 462: 347–361.
Krab, K., and M. Wikstrom. 1978. Proton translocating cytochrome c oxidase in artificial phospholipid vesicles. Biochim. Biophys. Acta 504: 200–214.
Casey, R. P., M. Thelen, and A. Azzi. 1979. Dicyclohexylcar- bodiimide inhibits proton translocation by cytochrome c oxidase. Biochem. Biophys. Res. Commun. 87: 1044–1051.
Martonosi, A. 1972. Biochemical and clinical aspects of sarcoplasmic reticulum function. Curr. Top. Membr. Transp. 3: 87–197.
Martonosi, A. 1968. Sarcoplasmic reticulum. IV. Solubilization of microsomal adenosine triphosphatase. J. Biol. Chem. 243: 71–81.
MacLennan, D. H. 1970. Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. J. Biol. Chem. 245: 4508–4518.
Pick, U., and E. Racker. 1979. Inhibition of the (Ca2 +) ATPase from sarcoplasmic reticulum by decyclohexylcarbodiimide: Evidence for location of the Ca2 + binding site in a hydrophobic region. Biochemistry 18: 108–113.
le Maire, M., J. V. Moller, and C. Tanford. 1976. Retention of enzyme activity by detergent solubilized sarcoplasmic reticulum Ca2 +-ATPase. Biochemistry 15: 2336–2342.
Racker, E. 1972. Reconstitution of a calcium pump with phos-pholipids and a purified Ca2 + -adenosine triphosphatase from sarcoplasmic reticulum. J. Biol. Chem. 247: 8198–8200.
Knowles, A. F., and E. Racker. 1975. Properties of a reconstituted calcium pump. J. Biol. Chem. 250: 3538–3544.
Zimniak, P., and E. Racker. 1978. Electrogenicity of Ca2 + transport catalyzed by the Ca2 +-ATPase from sarcoplasmic reticulum. J. Biol. Chem. 253: 4631–4637.
Hazelbauer, G. L., and J.-P. Changeaux. 1974. Reconstitution of a chemically excitable membrane. Proc. Nat. Acad. Sci. USA 71: 1479–1483.
Michealson, D. M., and M. A. Raftery. 1974. Purified acetylcholine receptor: Its reconstitution to a chemically excitable membrane. Proc. Nat. Acad. Sci. USA 71: 4768–4772.
McNamee, M. G., C. L. Weill, and A. Karlin. 1975. Purification of acetylcholine receptor from Torpedo californica and its incorporation into phospholipid vesicles. Ann. N.Y. Acad. Sci. 264: 175–182.
Epstein, M., and E. Racker. 1978. Reconstituion of car- bamylcholine-dependent sodium ion flux and desensitization of the acetylcholine receptor from Torpedo californica. J. Biol. Chem. 253: 6660–6662.
Huganir, R. L., M. A. Schell, and E. Racker. 1979. Reconstitution of the purified acetylcholine receptor from Torpedo californica. FEBS Lett. 108: 155–160.
Killian, P. C., C. R. Dunlap, P. Mueller, M. A. Schell, R. L. Huganir, and, E. Racker. 1980. Reconstitution of acetylcholine receptor from Torpedo californica with highly purified phos-pholipids: Effect of a-tocopherol, phylloquinone, and other terpenoid quinones. Biochem. Biophys. Res. Commun. 93: 409–414.
Ochoa, E. L. M., A. W. Dalziel, and M. G. McNamee. 1983. Reconstitution of acetylcholine receptor function in lipid vesicles of defined composition. Biochim. Biophys. Acta 727: 151–162.
Criado, M., H. Eibl, andF. J. Barrantes. 1982. Effects of lipids on acetylcholine receptor: Essential need of cholesterol for maintenance of agonist-induced state transitions in lipid vesicles. Biochemistry 21: 3622–3629.
Wu, W. C. S., H. P. H. Moore, andM. A. Raftery. 1981. Quantitation of cation transport by reconstituted membrane vesicles containing purified acetylcholine receptor. Proc. Natl. Acad. Sci. USA 78: 775–779.
Lindstrom, J., R. Anholt, B. Einarson, A. Engel, M. Osame, and M. Montai. 1980. Purification of acetylcholine receptors, reconstitution into lipid vesicles and study of agonist induced cation channel regulation. J. Biol. Chem. 255: 8340–8350.
Reynolds, J. A., and A. Karlin. 1978. Molecular weight in detergent solution of acetylcholine receptor from Torpedo californica. Biochemistry 17: 2035–2038.
Karlin, A. 1980. Molecular properties of nicotinic acetylcholine receptors. In: Cell Surface Reviews. C. W. Cotman, G. Poste, and G. L. Nicholson, eds. Elsevier/North-Holland, Amsterdam, pp. 191–260.
Huginar, R. L., and E. Racker. 1980. Endogenous and exogenous proteolysis of the acetylcholine receptor from Torpedo californica. J. Supramol. Struct. 14: 13–19.
Raftery, M. A., M. W. Hunkapillar, C. D. Strader, and L. E. Hood. 1980. Acetylcholine receptor: Complex of homologous sub- units. Science 208: 1454–1456.
Noda, M., H. Takahashi, T. Tanabe, M. Toyosato, Y. Furutini, T. Hirose, M. Asai, S. Inayama, T. Miyata, and S. Numa. 1982. Primary structure of a-subunit precursor of Torpedo californica acetylcholine receptor deduced from cDNA sequence. Nature (London) 299: 793–797.
Noda, M., H. Takahashi, T. Tanabe, M. Toyosato, S. Kikyotani, T. Hirose, M. Asai, M. Takashima, S. Inayama, T. Miyata, and S. Numa. 1983. Primary structures of p- and 7-subunit precursors of Torpedo californica acetylcholine receptor deduced from cDNA sequences. Nature (London) 301: 251 - 255.
Hoffmann, F. M. 1979. Solubilization and reconstitution of dopamine-sensitive adenylate cyclase from bovine caudate nucleus. J. Biol. Chem. 254: 255–258.
Hoffmann, F. M. 1979. A new method for removing nonionic detergent that allows reconstitution of dopamine-sensitive adenylate cyclase. Biochem. Biophys. Res. Commun. 86: 988–994.
Kanner, B. I. 1978. Solubilization and reconstitution of the 7- aminobutyric acid transporter from rat brain. FEBS Lett. 89: 47–50.
Kramer, R., and M. Klingenberg. 1979. Reconstitution of adenine nucleotide transport from beef heart mitochondria. Biochemistry 18: 4209–4215.
Miyamoto, H., and E. Racker. 1980. Solubilization and partial purification of the Ca2 + /Na+ antiporter from the plasma membrane of bovine heart. J. Biol. Chem. 255: 2656–2658.
Hirata, H., S. Nobuhito, Y. Masasuke, and Y. Kagawa. 1977. Isolation of the alanine carrier from the membranes of a thermophilic bacterium and its reconstitution into vesicles capable of transport. J. Supramol. Struct. 6: 77–84.
Fairclough, P., P. Malathi, H. Preiser, and R. K. Crane. 1979. Reconstitution into liposomes of glucose active transport from rabbit renal proximal tubule. Biochim. Biophys. Acta 553: 295–306.
Rothstein,A.,Z.T.Cabantchik,M.Balshin,andR.Juliano. 1975. Enhancement of anion permeability in lecithin vesicles by hydro-phobic protein extracted from red cell membranes. Biochem. Biophys. Res. Commun. 64: 144–150.
Newman, M. J., D. L. Foster, T. H. Wilson, and H. R. Kaback. 1981. Purification and reconstitution of functional lactose carrier from Escherichia coli. J. Biol. Chem. 256: 11804–11808.
Tank, D. W., C. Miller, and W. W. Webb. 1982. Isolated-patch recording from liposomes containing functionally reconstituted chloride channels from Torpedo electroplax. Proc. Natl. Acad. Sci. USA 79: 7749–7753.
Lin, S., and Spudich, J. A. 1974. Binding of cytochalasin B to a red cell membrane protein. Biochem. Biophys. Res. Commun. 61: 1471–1475.
Jung, C. Y., and L. M. Carlson. 1975. Glucose transport carrier in human erythrocyte membranes. J. Biol. Chem. 250: 3217–3220.
Kasahara, M., and P. C. Hinkle. 1976. Reconstitution of D-glucose transport catalyzed by a protein fraction from human erythrocytes in sonicated liposomes. Proc. Natl. Acad. Sci. USA 73: 396–400.
Kasahara, M., and P. C. Hinkle. 1977. Reconstitution and purification of the D-glucose transporter from human erythrocytes. J. Biol. Chem. 252: 7384–7390.
Kahlenberg, A., and C. A. Zala. 1977. Reconstitution of D-glucose transport in vesicles composed of lipids and intrinsic protein (zone 4.5) of the human erythrocyte membrane. J. Supramol. Struct. 7: 287–300.
Wheeler, T. J., and P. C. Hinkle. 1981. Kinetic properties of the reconstituted glucose transporter from human erythrocytes. J. Biol. Chem. 256: 8907–8914.
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Dubinsky, W.P. (1986). The Study of Transport and Enzymatic Processes in Reconstituted Biological Systems. In: Andreoli, T.E., Hoffman, J.F., Fanestil, D.D., Schultz, S.G. (eds) Physiology of Membrane Disorders. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2097-5_10
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DOI: https://doi.org/10.1007/978-1-4613-2097-5_10
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