Effects of Adenylate Mixtures on NAD-Malic Enzyme with limiting and saturating substrate and activator concentrations

Range Table - link
Organism C4 plants
Reference Furbank RT, Agostino A, Hatch MD. Regulation of C4 photosynthesis: modulation of mitochondrial NAD-malic enzyme by adenylates. Arch Biochem Biophys. 1991 Sep289(2):376-81PubMed ID1898077
Method NAD-malic enzyme was partially purified from bundle sheath cells of Atriplex spongiosa. Enzyme from Urochloa panicoides was purified according to Burnell (9) and appeared as a single band on SDS-polyacrylamide gels. NAD-malic enzyme activity was assayed spectrophotometrically as an absorbance increase at 340 nm in a 1-ml reaction as described in text. Enzyme was preincubated with the reaction mix for 1 to 2 minutes by malate addition prior to initiation of the assay by malate addition.
Comments The table compares the effect of various adenylates and oher phosphorylated compounds on NAD-malic enzyme activity with either limiting concentrations of both malate and the activator CoA (chosen to give about half maximal rates), or with saturating activator and substrates.
Entered by Uri M
ID 103981