Proteolytic activity of bacteria isolated from the oral cavities of BALB/c mice toward salivary proteins.
The proteolytic activities of 350 bacterial isolates from different sites (saliva, tongue, teeth, and mucosa) of the oral cavities of BALB/c mice were tested against different proteins found in saliva (immunoglobulins A, M, G, albumin, lysozyme, mucin, lactoferrin, and lactoperoxidase), some of which are considered to possess antibacterial activity. The results indicate that: (1) lysozyme, lactoferrin, and lactoperoxidase are hydrolyzed by from 46 to 70% of the indigenous flora of the oral cavities of BALB/c mice; (2) IgA and IgM appeared less sensitive to the proteolytic activities of these strains than did the other proteins tested; (3) the colonization of the oral cavity does not seem to be correlated with the proteolytic activity; and (4) the presence of specific Ig proteases is relatively scarce within this population.
D000818:Animals; D001419:Bacteria / Q000378:metabolism*; D007136:Immunoglobulins / Q000378:metabolism; D007781:Lactoferrin / Q000378:metabolism; D007784:Lactoperoxidase / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D009055:Mouth / Q000382:microbiology*; D009077:Mucins / Q000378:metabolism; D009113:Muramidase / Q000378:metabolism; D011489:Protein Denaturation; D012471:Salivary Proteins and Peptides / Q000378:metabolism*
D007136:Immunoglobulins; D009077:Mucins; D012471:Salivary Proteins and Peptides; D007784:Lactoperoxidase; D009113:Muramidase; D007781:Lactoferrin