Abstract
Horse liver alcohol dehydrogenase (LADH; EC 1.1.1.1) is today one of the most thoroughly investigated enzymes. Since its crystallization in 1948 (1) many authors have studied its properties in great details: the Swedish school, first with Theorell and then with Brändén and their co-workers, has extensively reviewed our knowledges on this and related dehydrogenases (2, 3). The active form of LADH is known to be dimeric and its three-dimensional structure has been solved at 2.4 Å resolution (4).
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© 1980 Plenum Press, New York
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Favilla, R., Mazzini, A. (1980). Polyfunctionality of Horse Liver Alcohol Dehydrogenase. In: Borsellino, A., Omodeo, P., Strom, R., Vecli, A., Wanke, E. (eds) Developments in Biophysical Research. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1077-8_29
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DOI: https://doi.org/10.1007/978-1-4684-1077-8_29
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