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- W2003250123 abstract "Intra- and inter-isozymic molecular relationships of mouse lactate dehydrogenase (EC 1.1.1.27) have been studied using starch-gel electrophoresis. 1. Each isozyme (LDH 2 to LDH 5) exhibits several narrow bands (sub-bands). These sub-bands present sequential and reversible molecular transformations inside the corresponding isozymic region of migration. 2. Several physicochemical factors, in vitro, determine the direction of these molecular transformations. 3. There are, in cells and tissues, definite specific properties, which are depending on the type of cellular differentiation, and which modify the behavior of the intra-isozymic sub-bands. 4. The enzymatic form migrating towards the cathode (cathodic band) may release, under certain conditions, the isozymes LDH5, LDH4, LDH3. This enzymatic form would appear to be an aggregation between isozymes. There is a relationship between cathodic band formation and the intra-isozymic sub-band transformations. A hypothesis according to which different molecular conformations of lactate dehydrogenase would account for these results, to a first approximation, is discussed." @default.
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- W2003250123 title "Transformations moleculaires au niveau des isozymes de la lacticodehydrogenase de la souris, mises en evidence par electrophorese en gel d'amidon" @default.
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- W2003250123 doi "https://doi.org/10.1016/0926-6593(66)90171-8" @default.
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