We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences. The deduced amino acid sequence from the human clone showed sequence identity to both the α and β subunits of the rat enzyme. The human enzyme is encoded as a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx. 19.5 (α) and 15 (β) kDa. A charge enriched region is present at the predicted site where cleavage occurs. Using polyclonal antibodies against the α and β subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
