Peroxidase-catalyzed oxidation of iodide in human saliva leads to the formation of a brown product with lambda max 287 nm and 353 nm (I3-) identified by the method of UV-spectrophotometry. I3- directly reacts with starch producing the characteristic blue complex. Salivary iodide peroxidase activity was found to be from 1.2 to 2.3 times higher then the activity of salivary peroxidases with natural substrates (SCN- and Cl-). Optimum for the iodide peroxidase activity in human saliva was found to be near pH 5.8. Salivary iodide peroxidase activity progressively lowers with the rise of pH value of the reaction mixture until total loss at the pH>7.4 was observed. Iodide peroxidase activity in human saliva at pH>7.4 is masked due to decomposition of I3- with the increase of pH along with the inhibition of peroxidases and I3- reduction by low molecular weight dialyzable salivary components possibly by Cl- and NCS-. Salivary iodide peroxidase activity was completely inhibited by peroxidase inhibitors (NaN3, 2-mercaptoethanol, thiourea), while addition of the peroxidase alternative substrates (ascorbate, quercetin, thiocyanate) resulted in partial inhibition of iodide peroxidase activity. The results of the study confirm the idea, that high activity of human saliva peroxidase with iodide as a substrate may play a crucial role in the bioavailability and metabolism of biologically active iodide.