Abstract
l-Alanine aminotransferase was demonstrated in a range of gastrointestinal, free-living and entomophagous nematodes. As in mammals, nematode l-alanine aminotransferase was found to exist in the form of mitochondrial and cytosolic isoenzymes. Whilst the majority of nematode enzymes exhibited a greater overall capacity for l-alanine synthesis than for l-alanine catabolism in vitro, the opposite was true for rat liver l-alanine aminotransferase. In contrast with rat liver, certain gastrointestinal nematodes were apparently able to transaminate d-alanine at low rates. H. contortus cytosolic l-alanine aminotransferase differed significantly from the mammalian enzyme with respect to both thermal stability and response to potential protective reagents.
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