Abstract
THE two different polypeptide units, M and H, of lactate dehydrogenase (LDH) are combined in tetrads to form the active enzyme molecules. Five different isoenzymes, LDH-1 (H4), LDH-2 (H3M), LDH-3 (H2M2), LDH-4 (HM3) and LDH-5 (M4), exist. The production of each subunit is under the control of a specific gene, one for the H and the other for the M polypeptide1. Normally, in a given species, the LDH isoenzyme pattern of each tissue is quite well defined and to some extent characteristic of that tissue. Distribution studies of this isoenzyme system should therefore give an indication of gone expression in experimental conditions.
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LATNER, A., LONGSTAFF, E. Modification by Crude Histones of Gene Activity for Lactate Dehydrogenase. Nature 224, 71–73 (1969). https://doi.org/10.1038/224071a0
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DOI: https://doi.org/10.1038/224071a0
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