Proteinases released during in vitro maintenance of third (L3) and fourth larval stage (L4) and adult Teladorsagia circumcincta (formerly Ostertagia circumcincta), an ovine abomasal nematode parasite, were characterized on the basis of pH optima, molecular size and specific proteinase inhibitor sensitivity. Enzyme activity was maximal at alkaline pH and stage-specific release was demonstrated. Proteinases released by the adult parasite degraded a variety of protein substrates including plasminogen, albumin and haemoglobin, in a pH-dependent manner. At alkaline pH fibrinogen degradation was restricted to the α and β peptide chains although the γ peptide chain was also degraded at acidic pH. Inhibitor sensitivity studies indicated that degradation was predominantly due to metalloproteinases although aspartyl proteinase activity was indicated at acidic pH.
