Zusammenfassung
Viele Proteine bestehen aus Untereinheiten: aus Polypeptiden, die durch Disulfidbrücken oder nichtkovalent zu einer definierten Struktur zusammengehalten werden. Bei Homooligomeren sind die Untereinheiten identisch, bei Heterooligomeren verschieden. Homooligomer sind z.B. die Enzyme Katalase und Aldolase (beide vier Untereinheiten), heterooligomer sind Neurotransmitter-Rezeptoren wie der Acetylcholin-Rezeptor (fünf Untereinheiten α2βγδ) oder spannungsabhängige K+ -Kanäle (acht Untereinheiten).
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Literatur
Lustig, A. et al. (2000): Molecular weight determination of membrane proteins by sedimentation equilibrium at the sucrose or Nycodenzadjusted density of the hydrated detergent micelle. BBA 1464, 199–206
Machaidze, G. & Lustig, A. (2006): SEGAL, a semiautomatic program for fitting sedimentation equilibrium patterns from analytical ultracentrifugation. J. Biol. Phys. Chem. 6, 91–102
Deisenhofer, J. et al. (1985): Structure of the proteins subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 A resolution. Nature 318, 618–624
Cooper, E. et al. (1991): Pentameric structure and subunit stoichiometry of a neuronal nicotinic acetylcholine receptor. Nature 350, 235–238
Lebherz, H. & Rutter, W. (1969): Distribution of fructose diphosphate aldolase variants in biological systems. Biochemistry 8, 109–121
MacKinnon, R. (1991): Determination of the subunit stoichiometry of a voltageactivated K + channel. Nature 350, 232–235
Penhoet, E. et al. (1967): The subunit structure of mammalian fructose diphosphate aldolase. Biochemistry 6, 2940–2949
Kobashi, K. (1968): Catalytic oxidation of sulfhydryl groups by ophenanthroline copper complex. BBA 158, 239–245
Zhang, M. & Kaltashov I.A. (2006): Mapping of Protein Disulfide Bonds Using Negative Ion Fragmentation with a Broadband Precursor Selection. Anal. Chem. 78, 4820–4829
Rehm, H. et al. (1986): Molecular characterization of synaptophysin, a major calcium binding protein of the synaptic vesicle membrane. EMBO J. 5, 535–541
Thomas, L. et al. (1988): Identification of synaptophysin as a hexameric channel protein of the synaptic vesicle membrane. Science 242, 1050–1053
Johnston, P. & Südhof, T. (1990): The multisubunit structure of synaptophysin; relationship between disulfide bonding and homo-oligomerization. J. biol. Chem. 265, 8869–8873
Arthur, C. & Stowell, M. (2007): Structure of synaptophysin: A hexameric MARVEL domain channel protein. Structure 15, 707–714
Hansen, R. et al. (2007): Quantification of protein thiols and dithiols in the picomolar range using sodium borohydride and 4,4’-dithio-dipyridine. Anal. Biochem. 363, 77–82
Darawshe, S. et al. (1987): Quaternary structure of erythrocruorin from the nematode Ascaris suum. Biochem. J. 242, 689–694
Waheed, A. et al. (1990): Quaternary structure of the Mr 46 000 mannose 6-phosphate specific receptor: effect of ligand, pH, and receptor concentration on the equilibrium between dimeric and tetrameric receptor. Biochemistry 29, 2449–2455
Darawshe, S. & Daniel, E. (1991): Molecular symmetry and arrangement of subunits in extracellular hemoglobin from the nematode Ascaris suum. Eur. J. Biochem. 201, 169–173
Hucho, F. et al. (1975): Investigation of the symmetry of oligomeric enzymes with bifunctional reagents. Eur. J. Biochem. 59, 79–87
Klotz, I. et al. (1970): Quaternary structure of proteins. Ann. Rev. Biochem. 39, 25–62
Gaffney, B. (1985): Chemical and biochemical crosslin-king of membrane components. BBA 822, 289–317
Hucho, F. et al. (1978): The acetylcholine receptor as part of a protein complex in receptor-enriched membrane fragments from Torpedo californica electric tissue. Eur. J. Biochem. 83, 335–340
Langosch, D. et al. (1988): Conserved quaternary structure of ligand-gated ion channels: The postsynaptic glycine receptor is a pentamer. Proc. Natl. Acad. Sci. USA 85, 7394–7398
Kapp, O. et al. (1990): Calculation of subunit stoichiometry of large multisubunit proteins from amino acid compositions. Anal. Biochem. 184, 74–82
Pestka, et al. (1983): Specific immunoassay for protein dimers, trimers and higher oligomers. Anal. Biochem. 132, 328–333
Whiting, P. et al. (1987): Neuronal nicotinic acetylcholine receptor β-subunit is coded for by the cDNA clone α4. FEBS lett. 219, 459–463
Li, M. et al. (1992): Specification of subunit assembly by the hydrophilic amino-terminal domain of the shaker potassium channel. Science 257, 1225–1230
Maniolos, M. (1990): Transmembrane helical interactions and the assembly of the T cell receptor complex. Science 249, 274–277
Pakula, A. & Simon, M. (1992): Determination of transmembrane protein structure by disulflide cross-linking: the E. coli Tar receptor. Proc. Natl. Acad. Sci. USA 89, 4144–4148
Sumikawa, K. (1992): Sequences on the N-terminus of Ach receptor subunits regulate their assembly. Mol. Brain Res. 13, 349–353
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Rehm, H., Letzel, T. (2010). Untereinheiten. In: Der Experimentator: Proteinbiochemie/Proteomics. Experimentator. Spektrum Akademischer Verlag. https://doi.org/10.1007/978-3-8274-2313-9_8
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