Antibacterial activity of the purified peroxidase from human parotid saliva.
The peroxidase of human parotid saliva has been purified by concentration, gel filtration on Sephadex G-200, and ion exchange chromatography on Amberlite CG-50. The purified product was devoid of amylase activity, lysozyme activity, and immunoglobulin A (IgA). However, it had an inhibitory effect on the growth of Lactobacillus acidophilus in complete growth medium and on lysine accumulation by L. acidophilus in a buffer-glucose medium, when combined with thiocyanate ions. The concentrations of peroxidase and thiocyanate ions employed were within the range found in saliva. The fractions which contained IgA did not have an anti-bacterial effect on L. acidophilus under the conditions employed. Parotid saliva also contained low molecular weight inhibitors of peroxidase activity. These studies support the involvement of the salivary peroxidase in an antibacterial system in saliva.
D000328:Adult; D000681:Amylases / Q000032:analysis; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006801:Humans; D005779:Immunodiffusion; D007779:Lactobacillus acidophilus / Q000187:drug effects*; D009113:Muramidase / Q000032:analysis; D010306:Parotid Gland; D010544:Peroxidases / Q000302:isolation & purification / Q000494:pharmacology*; D012463:Saliva / Q000032:analysis / Q000201:enzymology*; D005719:gamma-Globulins / Q000032:analysis
D005719:gamma-Globulins; D010544:Peroxidases; D000681:Amylases; D009113:Muramidase