Vortex-mixing-induced inactivation of arginine-specific ADP-ribosyltransferase activity and re-activation of the less-active form by dithiothreitol plus NaCl under anaerobic conditions.
We observed dilution/vortex-mixing-induced inactivation of arginine-specific ADP-ribosyltransferase purified from chicken peripheral polymorphonuclear granulocytes (heterophils) and re-activation of the less active form by dithiothreitol plus NaCl, under anaerobic conditions. The vortex-mixing-induced inactivation of the diluted enzyme was rapid; more than 85% of the enzyme activity was lost with 1-min vortex-mixing at room temperature. When the less-active form of the enzyme was treated with 10 mM dithiothreitol plus 0.2 M NaCl, under anaerobic conditions, more than 50% of the enzyme activity was restored. Putative mechanisms of the vortex-mixing-induced inactivation and dithiothreitol/NaCl-dependent re-activation of the arginine-specific ADP-ribosyltransferase are discussed.
Department of Biochemistry, Shimane Medical University, Izumo, Japan.
T
T
Ohno
M
M
Badruzzaman
Y
Y
Nishikori
M
M
Tsuchiya
J
J
Jidoi
M
M
Shimoyama
D036002:ADP Ribose Transferases / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism*; D000693:Anaerobiosis; D000818:Animals; D002498:Centrifugation; D002645:Chickens; D004229:Dithiothreitol / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D004793:Enzyme Reactivators / Q000494:pharmacology*; D006098:Granulocytes / Q000201:enzymology; D012965:Sodium Chloride / Q000494:pharmacology*
D004793:Enzyme Reactivators; D012965:Sodium Chloride; D036002:ADP Ribose Transferases; D004229:Dithiothreitol