Protein-phosphate complexes as an inhibitor of iron-induced lipid peroxidation.
Effect of phosphate buffer (pH 6.2) alone or in the presence of bovine serum albumin and other proteins on iron (II)-induced lipid peroxidation was studied. Phosphate buffer alone and in the presence of bovine serum albumin was found to inhibit lipid peroxidation. The inhibition was higher when bovine serum albumin was also present. Other proteins also inhibited lipid peroxidation in the presence of phosphate. Inhibition by proteins in the presence of phosphate seems to be due to binding of iron with phosphate and with protein-phosphate complexes. Reversal in inhibition was observed with an increase in iron concentration in reaction mixture. Equilibrium dialysis showed more binding of iron to protein in the presence of phosphate than in the presence of chloride ions.
Dawra
R K
RK
Biochemistry Laboratory, Indian Veterinary Research Institute, Palampur.
Sharma
O P
OP
Makkar
H P
HP
D000818:Animals; D002021:Buffers; D002614:Chelating Agents / Q000096:biosynthesis; D002712:Chlorides / Q000494:pharmacology; D007501:Iron / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D008054:Lipid Peroxides / Q000096:biosynthesis*; D008297:Male; D010084:Oxidation-Reduction; D010710:Phosphates / Q000494:pharmacology*; D011485:Protein Binding; D012661:Semen / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000494:pharmacology*; D013094:Spermatozoa / Q000187:drug effects* / Q000378:metabolism
D002021:Buffers; D002614:Chelating Agents; D002712:Chlorides; D008054:Lipid Peroxides; D010710:Phosphates; D012710:Serum Albumin, Bovine; D007501:Iron