The salt-induced dissociation and inactivation of a mammalian enolase: evidence for the formation of active monomers.
The gamma gamma isozyme of rabbit enolase was labeled with fluorescein and the effects of NaClO4 on both enzymatic activity and fluorescence polarization were studied. NaClO4, but not NaCl, dissociates and partially inactivates the enzyme. If dissociation is prevented, either by the addition of substrate or by covalently crosslinking the enzyme, inactivation is also prevented. Analysis of the time and concentration dependence of inactivation and dissociation shows that the decrease in activity is a two-step process: D in equilibrium 2M in equilibrium 2M*. Both monomeric forms of the enzyme are catalytically active.
Trepanier
D
D
Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec.
Wong
C
C
Kornblatt
M J
MJ
D000818:Animals; D001921:Brain / Q000201:enzymology; D002850:Chromatography, Gel; D006168:Guinea Pigs; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D009994:Osmolar Concentration; D010472:Perchlorates / Q000494:pharmacology*; D010751:Phosphopyruvate Hydratase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D017670:Sodium Compounds
D007527:Isoenzymes; D046911:Macromolecular Substances; D010472:Perchlorates; D017670:Sodium Compounds; C031068:sodium perchlorate; D010751:Phosphopyruvate Hydratase