R. Selvam et S. Devaraj, OXALATE BINDING TO RAT-KIDNEY MITOCHONDRIA - INDUCTION BY OXIDIZED GLUTATHIONE, Indian Journal of Biochemistry & Biophysics, 33(1), 1996, pp. 62-65
Increased oxalate binding with negative correlation with reduced gluta
thione content was observed during lipid peroxidation in rat kidney mi
tochondria. In presence of oxidized glutathione (GSSG), peroxidized mi
tochondria lost 48% of protein-SH with concomitant 3-fold increase in
oxalate binding activity while control mitochondria lost only 20% prot
ein-SH with only 0.8 fold increase in oxalate binding activity. The GS
SG-induced oxalate binding was apparently due to two-fold increased af
finity of oxalate to the protein. Reduced glutathione (GSH) inhibited
oxalate binding competitively with K-i, 1.4x10(-3) M. Urolithic rat ki
dney mitochondria showed 30-50% increase in oxalate binding activity a
long with depletion of GSH and protein-SH. These studies suggest that
oxalate binding is regulated by thiol status of mitochondria.