The presence of a proteolytic enzyme has been demonstrated in ground-up preparations of Schistosoma mansoni. A twenty-fold purification has been achieved by ultracentrifugation at pH 3.0; the enzyme has an optimum pH of 3.9 and a marked substrate specificity for haemoglobin. No significant proteolysis was observed either with whole serum at pH values of 3.9, 6.0 or 8.0, or with isolated serum proteins at pH ranges between 2.5 and 7.7. The evidence is discussed that this enzyme may be located in the intestine of the schistosomes and that it is, at least in part, responsible for the supply of amino acids to the organisms.Little is known about the protein metabolism of Schistosoma mansoni.Rogers (1940) reported that the black pigment present in the intestine of S. mansoni is probably haematin formed by the digestion of haemoglobin from the host. The parasite must obtain nutrient materials, including amino acids, from the blood of the host, and it is conceivable that there is a mechanism for the degradation of one or more blood proteins, following ingestion into the intestine of the parasite. Halawani, Hafez, Newsome, and Cooper (1949) observed that haemoglobin disappeared from the medium in which S. mansoni survived in vitro.If it were known precisely what amino acids are required by S. mansoni and by what mechanism the parasite obtains them, an opportunity might become available for the development of schistosomicidal drugs. An initial approach to this problem is reported in this paper, in which the demonstration, partial purification and properties of a proteolytic enzyme from S. mansoni are described. The enzyme shows a marked specificity for haemoglobin (Timms and Bueding, 1958).METHODS AND MATERIALS Survival Studies.-Survival of schistosomes in a synthetic medium was studied by the use of procedures reported previously (Ross and Bueding, 1950). The synthetic medium used in the present investigation contained the following constituents in