Studies on alanine aminotransferase in nematodes.

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.

Cite this paper

@article{Walker1991StudiesOA, title={Studies on alanine aminotransferase in nematodes.}, author={Jacquae Walker and John E. Barrett}, journal={International journal for parasitology}, year={1991}, volume={21 3}, pages={377-80} }