Abstract
The colour change that takes place in solutions of hemoproteins when enzyme-substrate complexes are formed1, 2, 3 or when the prosthetic group combines with the apoprotein4, 5 has caused these enzyme complex formations to be eagerly studied. The spectral change that takes place at the same time made possible an intensive study of the reaction kinetics of these enzymes6, 7.
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
Stern, K. G.: J. of Biol. Chem. 114, 473 (1936).
Keilin, D., and T. Mann: Proc. Roy. Soc. London 122 B, 119 (1936).
Chance, B.: Acta chem. scand. (Copenh.) 1, 236 (1947).
Theorell, H.: Arkiv. Kemi 14B, No. 20 (1940).
Theorell, H., and A. Maehly: Acta chem. scand. (Copenh.) 4, 422 (1950).
Chance, B.: In The Enzymes, 2, Part 1 (j. B. Summer and K. Myrbäck Ed.) Academic Press, Inc. New York, N. Y.
Chance, B.: In Modern Trends in Biochemistry and Physiology., Academic Press, Inc. New York.
Warburg, O., and W. Christian: Biochem. Z. 298, 368 (1938).
Morell, D. B.: Biochemic. J. 51, 657 (1952).
Kuhn, R., and P. Boulanger: Ber. 69, 1557 (1936).
Kuhn, R., and Th. Wagner-Jauregg: Ber. 67, 361 (1934).
Michaelis, L., M. P. Schubert and C. V. Smythe: J. of Biol. Chem. 116, 587 (1936).
Haas, E.: Biochem. Z. 290, 291 (1937).
Bonnichsen, R.: Acta chem. scand. (Copenh.) 4, 714 (1950).
Warburg, O., W. Christian and A. Griese: Biochem. Z. 282, 157 (1935).
Karrer, P., and F. Benz: Helvet. chim. Acta 19, 1028 (1936).
Bonnichsen, R.: Acta chem. scand. (Copenh.) 4, 715 (1950).
Bonnichsen, R., and H. Theorell: See H. Theorell, 8e Conseil de Chimie de l’Institut International de Solvay Bruxelles 1950, p. 398.
Theorell, H., and R. Bonnichsen: Acta chem. scand. (Copenh.) 5, 1105 (1951).
Chance, B., and J. B. Neilands: J. of Biol. Chem. 199, 373 (1952).
Chance, B.: Federat. Proc. 11, No. 1 (1952).
Chance, B.: Nature (Lond.) 169, 215 (1952).
Hogeboom, G. H., and W. C. Schneider: J. of Biol. Chem. 197, 611 (1952).
Theorell, H., and R. Bonnichsen: Acta chem. scand. (Copenh.) 5, 329 (1951).
Krimsky, J., and E. Racker: J. of Biol. Chem. 198, 721 (1952).
Racker, E., and J. Krimsky: J. of Biol. Chem. 198, 731 (1952).
Barron, G. E. S., and Sumner Levine: J. of Biol. Chem. 41, 174 (1952).
Meyerhof, G., P. Ohlmeyer and W. Möhle: Biochem. Z. 297, 90 (1938).
Colowick, S. P., N. O. Kaplan and M. M. Ciotti: J. of Biol. Chem. 191, 447 (1951).
Feigelson, P., J. N. Williams jr. and C. A. Elvehjem: J. of Biol. Chem. 189, 361 (1951).
Alivasatos, G. A. S., and O. F. Denstedt: J. of Biol. Chem. 199, 493 (1952).
Maynard, E., Pulman, P. S. Colowick and N. O. Kaplan: J. of Biol. Chem. 194, 593 (1952).
Negelein, E., and H. J. Wulff: Biochem. Z. 293, 351 (1937).
Backer, E.: J. of Biol. Chem. 184, 313 (1952).
Neilands, J. B.: J. of Biol. Chem. 199, 373 (1952).
Theorell, H., and B. Chance: Acta chem. scand. (Copenh.) 5, 1127 (1951).
Bliss, A.: Biol. Bull. 97, 221 (1949).
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1953 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Bonnichsen, R. (1953). The Mode of Operation of Dehydrogenases with Special Reference to Alcohol Dehydrogenase. In: Biologie und Wirkung der Fermente. Colloquium der Gesellschaft für Physiologische Chemie am 17./18. April 1953 in Mosbach/Baden, vol 4. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-85780-5_7
Download citation
DOI: https://doi.org/10.1007/978-3-642-85780-5_7
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-01683-0
Online ISBN: 978-3-642-85780-5
eBook Packages: Springer Book Archive