Abstract
Asparaginase, which catalyses the conversion of asparagine to ammonia and aspartate, has been purified from maturing Lupinus seeds. The enzyme has a high K m for asparagine (12.2 mM) and is able to utilise a number of asparagine analogues as substrates although glutamine and its analogues are not reactive. The possible route for the reassimilation of the liberated ammonia is discussed.
Sign-in/Register to access full text options 
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.
