Proteolytic activities in the supragingival plaque of monkeys (Macaca fascicularis).

Thirteen peptidase substrates were hydrolysed by this plaque. After fasting the monkeys for 24 h, the rates of hydrolysis of N-leucyl-, N-alanyl-, N-isoleucyl- and N-tyrosyl-2-naphthylamines, glycyl-L-proline 4-nitroanilide, N alpha-benzoyl-DL-arginine-2-naphthylamine and L-leucyglycine were significantly increased. Changes in these peptidase activities may serve to enhance the mobilization of amino acids and peptides, and they may explain why the growth rates of dental-plaque bacteria in vivo are generally unaffected by the availability of the host's diet.