Proteinase activity in rheumatoid arthritis

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Proteolytic activity amongst selected Saprolegnia species

Saprolegia ssp. effectively utilized the protein casein as a sole source of carbon, nitrogen and sulphur, indicating considerable proteolytic activity. In the presence of a more simple carbon source such as glucose, which was readily assimilated, catabolite repression was not observed and casein exploitation was enhanced. Free proteinase activity was not detected by a number of methods, irrespective of culture conditions. However, clearing by mycelia of skimmed milk agar or agar amended with bacteria demonstrated a close association between proteinases and hyphae, suggestive of natural immobilization of proteinases. Casein breakdown was accompanied by release of individual amino acids and ammonia. The latter, indicative of amino acid assimilation and metabolism, was also associated with an increase in pH of culture medium. Single amino acids did not support growth of Saprolegnia but in combination with other amino acids, methionine encouraged greatest biomass production. Certain groupings of amino acids affected growth in a manner which departed from that expected, as assessed by multifactorial analysis of variance, and either enhanced or reduced growth.