Abstract
ADP could efficiently replace ATP in the 6-phosphofructokinase (ATP: D-fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.11)) reaction catalysed by a highly purified enzyme preparation from banana. A 28-fold purification of the enzyme devoid of other interfering enzymes like adenylkinase (AK), aldolase, pyrophosphate fructose-6-phosphate phosphotransferase (PFP) and lactic dehydrogenase (LDH) was achieved. Maximum activity was observed with 0.5 mM ADP and K m value for ADP was 167 μM. Polyethyleneimine cellulose thin layer chromatography of nucleotide products confirmed the utilization of ADP for the phosphorylation of fructose-6-phosphate (F6P) by the enzyme releasing AMP as product.
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.
