Abstract
The presence of argininosuccinate lyase (ASL), an enzyme catalyzing the final step of arginine biosynthesis, was demonstrated in the heterocystous cyanobacterium Nostoc PCC 73102 by measuring in vitro enzyme activity and by visualization of ASL in native protein gels. Activity staining of a native PAGE gel revealed one ASL-dependent band with a molecular mass of about 240 kDa. A colorimetric assay for ASL based on the measurement of urea produced from arginine in the presence of an excess of arginase was further used to analyze the cyanobacterial ASL. The in vitro ASL activity was highest in cells in exponential growth phase and decreased significantly during the stationary phase of growth, ranging from 4.4 to 0.8 nmol of product formed (mg protein)-1 min-1. Including arginine, citrulline or ornithine in the growth medium resulted in no significant change in the ASL activities, indicating that Nostoc PCC 73102 ASL is not regulated by metabolites of the ornithine cycle.
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.
