Abstract
Pyrimidine nucleoside monophosphate kinase was purified from baker's yeast to 280-fold. The molecular weight of the enzyme was calculated to be 26, 000 by gel filtration. With ATP as a phosphate donor, UMP was the most active phosphate acceptor. Besides UMP, the kinase also phosphorylated CMP, dCMP and dUMP. Km values for UMP, CMP, dCMP and dUMP were 0.052, 0.071, 0.54 and 8.5mM, respectively. The kinase was activated by preincubation with dithiothreitol. The extent of the activation depended on the concentration of dithiothreitol and incubation time. HgCl2, p-CMB and N-ethylmaleimide inhibited this enzyme.
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.
