Abstract
The molecular weight of NAD-dependent dehydrogenases varies from some twenty thousands to some millions. Most of the molecular weights are in the range 50, 000 to 200, 000 (1). The subunit structure of the majority of dehydrogenases is now well established, most of them are composed of more than one polypeptide chain. All these enzymes consist of polypeptide chains with molecular weights between 14, 000 and 50, 000 (1, 2). In general only the associated molecule is observed in the native state. If this is the case it can be assumed that the self-assembly process to the associated and active molecule leads to such an important lowering of free energy that in the native state the equilibrium concentration of the single polypeptide chain is far below detectibility.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Sund, H., in Biological Oxidations (ed. by T.P. Singer), Interscience Publishers, New York — London 1968, p. 641.
Sund, H., and Weber, K., Angew. Chem., 78, 217 (1966);
Sund, H., and Weber, K., Angew. Chem. Intern. Ed., 5, 231 (1966).
Sund, H., Diekmann, H., and Walleniels, K., Advances in Enzymology, 26, 115 (1964).
Sund, H., Acta Chem. Scand., 17, S 102 (1963).
Olson, J.A., and Anfinsen, C.B., J. Biol. Chem., 197, 67 (1952).
Kubo, H., Yamano, T., Iwatsubo, M., Watari, H., Soyama, T., Shiraishi, J., Sawada, S., Kawashima, N., Mitani, S., and Ito, K., Bull. Soc. Chim. Biol., 40, 431 (1958).
Churchich, J.E., and Wold, P., Biochemistry, 2, 781 (1963).
Eisenberg, H., and Tomkins, G.M., J. Mol. Biol., 31, 37 (1968).
Sund, H., and Burchard, W., European J. Biochem., 6, 202 (1968).
Dessen, P., and Pantaloni, D., European J.Biochem., 8, 292 (1969).
Sund, H., in Mechanismen enzymatischer Reaktionen (14. Colloquium der Gesellschaft für Physiologische Chemie, 1963), Springer-Verlag, Berlin-Göttingen-Heidelberg 1964, p. 318.
Sund, H., Habilitationsschrift, Universität Freiburg 1964.
Sund, H., Angew. Chem., 76, 954 (1964);
Sund, H., Angew. Chem. Intern. Ed., 3, 802 (1964).
Sund, H., Pilz, I., and Herbst, M., European J.Biochem., 7, 517 (1969).
Sund, H., Acta Chem.Scand., 15, 940 (l96l).
Bayley, P.M., and Radda, G.K., Biochem. J., 98, 105 (1966).
Churchich, J.E., Biochim.Biophys.Acta, 147, 32 (1967).
Elias, H.G., and Bareiss, R., Chimia, 21, 53 (1967).
Colman, R.F., and Frieden, C., J.Biol.Chem., 241, 3661 (1966).
Frieden, C., J.Biol.Chem., 237, 2396 (1962).
Burchard, W., Markau, K., and Sund, H., unpublished results.
Chun, P.W., and Kim, S.J., Biochemistry 8, 1633 (1969).
Eisenkraft, B., van Dort, J.B., and Veeger, C., Biochim.Biophys.Acta, 185, 9 (1969).
Steiner, R.F., Arch.Biochem.Biophys., 39, 333 (1952).
Jirgensons, B., J. Am. Chem. Soc., 83, 3161 (1961).
Wolff, J., J.Biol.Chem., 237, 230 (1962).
Minssen M., Diplomarbeit, Universität Freiburg 1966.
Eisenberg, H., and Reisler, E., personal communication, see also this Symposium.
Valentine, R.C., Abstracts, 4th European Regional Conference on Electron Microscopy, Rome 1968, 2, 3.
Minssen M., and Sund, H., Abstracts, 6th Meeting of the European Biochemical Societies, Madrid 1969, Nr. 1072 (p. 330).
Marler, E., and Tanford, C., J.Biol.Chem., 239, 4217 (1964).
Frieden, C., J.Biol.Chem., 234, 815 (1959).
Frieden, C., J. Biol. Chem., 238, 146 (1963).
Frieden, C., and Colman, R.F., J.Biol.Chem., 242, 1705 (1967).
Tomkins, G.M., and Yielding, K.L., Cold Spring Harbor Symposia on Quantitative Biology, 26, 331 (l96l).
Tomkins, G.M., Yielding, K.L., Curran, J.F., Summers, M.R., and Bitensky, M.W., J.Biol.Chem., 240, 3793 (1965).
Bitensky, M.W., Yielding, K.L., and Tomkins, G.M., J.Biol.Chem., 240, 1077 (1965).
Eisenkraft, B., and Veeger, C., Biochim.Biophys.Acta, 167, 227 (1968).
Fisher, H.F., Mc Gregor, L.L., and Power, U., Biochim. Biophys. Res. Comm., 8, 402 (1962).
Karreman, G., Steele, R.H., and Szent-Györgyi, A., Proc. Nat. Acad. Sci. (US), 44, 140 (1958).
Velick, S.F., J.Biol.Chem., 233, 1455 (1958).
Förster, T., Fluoreszenz Organischer Verbindungen, Vandenhoeck and Ruprecht, Göttingen 1951.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1970 Springer-Verlag Berlin · Heidelberg
About this chapter
Cite this chapter
Krause, J., Markau, K., Minssen, M., Sund, H. (1970). Quaternary Structure and Enzymic Properties of Beef Liver Glutamate Dehydrogenase. In: Sund, H. (eds) Pyridine Nucleotide-Dependent Dehydrogenases. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-49974-6_25
Download citation
DOI: https://doi.org/10.1007/978-3-642-49974-6_25
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-49976-0
Online ISBN: 978-3-642-49974-6
eBook Packages: Springer Book Archive