Purification and kinetic properties of Mus booduga (Gray) hepatic arginase.
Hepatic L-arginase from the Mus booduga (Gray) was purified and its kinetic characteristics were investigated. The enzyme was not adsorbed on DEAE-cellulose, but was retained on CM-cellulose column at pH 7.2. The Michaelis-Menten constant was 8.3 mM for L-arginine and was independent of pH in the range of 7.5-10.5. L-arginine concentrations as high as 0.4 M did not exert substrate inhibition in the pH range 7.4-10.0. Manganese was required at a concentration of 0.05 M for full activation of the enzyme. L-ornithine and L-lysine inhibited the enzyme competitively with inhibitory constants of 1.9 mM and 3.7 mM respectively. Several properties of the L-arginase from Mus booduga clearly identify it as an enzyme similar to ureotelic basic arginases from mammalian liver.
Prasad
G V
GV
Department of Zoology, Sri Venkateswara University, Tirupati, India.
Lokanatha
V
V
Sreekanth
K
K
Rajendra
W
W
D000818:Animals; D001119:Arginase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004789:Enzyme Activation / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D051379:Mice; D009115:Muridae; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D001119:Arginase