Abstract
During 10 years after its crystallization (1, 1948) horse LADH was regarded as a homogeneous protein. While working with us in Stockholm, Dalziel (2, 19 58) in free boundary electrophoresis and chromatography observed a minor, more acidic component, that was also active with ethanol as substrate. Still more subfractions were observed by a Swiss group, von Wartburg, et al. (3, 4) and McKinley-McKee and Moss (5) using respectively agar or starch gel electrophoresis (1965–66).
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References
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Theorell, H. (1970). Structural and Functional Relationships between Isoenzymes of Horse LADH. In: Sund, H. (eds) Pyridine Nucleotide-Dependent Dehydrogenases. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-49974-6_10
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DOI: https://doi.org/10.1007/978-3-642-49974-6_10
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