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1. Three SOD isoenzymes obtained from purified extracts of Ascaris suum were characterized. 2. The physico-chemical characteristics studied were: optimum pH, methods of preservation of enzymatic activity, molecular weight, and the u.v. and visible light absorption spectra. 3. The optimum pH for the Cu, Zn SOD I and II was 10.2 and 10.1 for the Mn SOD. 4. The extracts retained their levels of activity longer at -70 degrees C, and after lyophilization. The Mn SOD was more labile than the Cu, Zn SOD I and II. 5. The molecular weights obtained by filtration through Sephadex G-75 were: 73,000 for Mn SOD; 42,600 for Cu, Zn SOD I; and 39,800 for the Cu, Zn SOD II. 6. Both the u.v. and visible light spectra were similar to other dismutases from other sources.

Muscle, hypodermis and gastrointestinal epithelial cells from adult female Ascaris lumbricoides var. suum were found to contain serotonin based upon glyoxylic acid induced histofluorescence and indirect immunolabeling with an antiserotonin monoclonal antibody conjugated to protein A-colloidal gold. Histofluorescence indicated that muscle-hypodermis and intestinal epithelial cells contained significant concentrations of 5-hydroxytryptamine while fluorescence was absent in the nerve cord and cuticle. Immunolabeling at the ultrastructural level indicated that serotonin was sequestered in electron-opaque patches, dense vesicles and mitochondria of the muscle-hypodermis and intestinal tissue. Perfusion of whole worms and isolated tissues with 10(4) M-serotonin further indicated: (1) immunolabeled patches and dense vesicles were often associated with cytoskeletal elements, (2) serotonin did not appear to enter the intestinal or muscle cells by endocytosis, (3) immunolabeled patches examined with energy dispersive X-ray spectrometry (X-ray microanalysis) were found to contain iron at concentrations approximately double that of the surrounding cytoplasm.

Extracts of various helminthic parasites were studied to determine the molecular carrier of the hapten phosphorylcholine (Pc). Physicochemical studies showed that the carrier was heterogeneous with regard to apparent molecular weight (70,000-greater than 10(6) daltons). Ultracentrifugal analysis of Ascaris suum and Nippostrongylus brasiliensis showed that Pc was associated with low (LDL), high (HDL) and a heterogeneous group of very high density (VHDL) lipoproteins. The majority of Pc was found in the most dense VHDL (d greater than 1.25 g ml-1). The apparent molecular weight and particle diameter of A. suum HDL was 751,000 daltons and 16.2 nm, respectively. The apparent molecular weights and particle diameters of A. suum VHDL ranged from 469,000 to 677,000 daltons and 13.6 to 15.5 nm, respectively. The electrophoretic mobilities of A. suum LDL and HDL were beta and gamma, respectively. A suum VHDL was electrophoretically heterogeneous. It is probable that Pc is associated with the phospholipid phosphatidylcholine.