Further studies on the purine phosphoribosyltransferase 'burst' velocity reaction.
In the assays used to determinate the adenine and hypoxanthine-guanine phosphoribosyltransferases activities from Artemia cysts two phases of velocity are observed in the synthesis of AMP, IMP and GMP: one initial burst and a second, slower, steady-state velocity. Both reaction velocities are divalent cation-dependent and temperature-resistant, as they are detectable at temperatures from 0 to 100 degrees C. Butanol, frequently employed to interrupt the purine phosphoribosyltransferase reactions, does not inhibit the enzyme activities. The 'burst' phase is not detected when the reaction is ended by the addition of EDTA. These data support that the initial velocities of these enzymatic reactions may be due to the accumulation of products formed by the overall reaction, developed subsequent to the controlled reaction period, being the 'burst' a result from the relative resistance of these enzymes to the agents that are often used to stop the reaction, such as heat or butanol.
Montero
C
C
Instituto de Investigaciones Biomédicas del C.S.I.C., Madrid, Spain.
Llorente
P
P
D000818:Animals; D001156:Artemia / Q000201:enzymology*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003600:Cytosol / Q000201:enzymology; D007041:Hypoxanthine Phosphoribosyltransferase / Q000378:metabolism; D007700:Kinetics; D010430:Pentosyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity; D013816:Thermodynamics
D010430:Pentosyltransferases; C022484:purine phosphoribosyltransferase; D007041:Hypoxanthine Phosphoribosyltransferase