Abstract
L-ASPARAGINASE (EC 3.5.1.1), which hydrolyses the amide group of asparagine, inhibits certain neoplasms1–4 and is used for treating human acute leukaemias5,6. Although asparaginase sequentially inhibits protein, RNA and DNA synthesis7, its cellular action is undefined. We have investigated the effects of asparaginase on the synthesis of carbohydrate–amino-acid linkages in glycoproteins which involve the amide group of asparagine and N-acetyl-glucosamine residues8. Our preparation of L-asparaginase (from Escherichia coli, 321–363 U/mg protein) was free of contaminating enzymatic activity, although it was slightly active (2.1 per cent of the activity towards asparagine) with glutamine as substrate. The preparation was free of glycosidase and proteolytic activities9,10.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
