Abstract
lysosomil and -microsoma1 marker enzymes xanthine dehydrogenase and glucose-6-phosphatase (less than 2% of the total activity in the extract). The amount of ALAT activity in this fraction was higher than this percentage and, consequently, was not due to contamination by cytosolic material. The total amount of ALAT activity in the other subcellular fractions represented less than 1.1% of the total activity in the extract and was in the same range as the cytosolic and mitochondrial marker enzymes. This activity is interpreted as being due to material from those fractions. These results agree with the values obtained for the enzyme of rat liver where more than 80% of the ALAT activity was present in the soluble fraction, but contrast with the distribution of the pig liver enzyme where the cytosolic and mitochondrial isoenzymes account for 46% and 54% of the total activity, respectively [S]. The important differences in the concentration of the two ALAT isoenzymes found in the liver from various origins can be explained by an independent regulation of their synthesis and degradation, or by a certain specialization with respect to their catalytic properties. This would be of different importance in the various origins studied, as occurs with a closely related and well-characterized enzyme, aspartate 1 .
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