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  • Title: Trypsin inhibitors from Ascaris: the reactive P1 site of the inhibitors (a correction) and location of the inhibitors and host trypsin in cross-sections of Ascaris.
    Author: Goodman RB, Martzen MR, Peanasky RJ.
    Journal: Acta Biochim Pol; 1983; 30(2):233-44. PubMed ID: 6408861.
    Abstract:
    Ascaris trypsin inhibitors 1, 2, and 3 have arginine at their reactive P1 site. This corrects an earlier report that lysine is the reactive P1 site residue in Ascaris trypsin inhibitor 1 (Peanasky et al., 1974, Bayer Symposium V: Proteinase Inhibitors, pp. 649-666). The present work illustrates that the residue modification method of Fritz et al. (1969, Z. Physiol. Chem., 350, 933-944) may not be reliably interpreted when trypsin inhibitors have an unusually high lysine content (greater than 12% of the molecular weight of the inhibitor). Thus the following procedure is recommended: treat the inhibitor with maleic anhydride first and second with butanedione reagent; then remove the maleyl groups in an acid environment and determine the activity of the inhibitor. Immunoperoxidase staining shows that antibody to Ascaris trypsin inhibitor 1 binds to body wall muscle, intestine, eggs and sperm in cross-sections of Ascaris. Antibody to TLCK-porcine trypsin binds to the same tissues and at the same sites as the antibody to Ascaris trypsin inhibitor 1. This is the first demonstration that a protein that originated in the host has been found in the parasite, Ascaris. Analyses of homogenates and of extracts of separated tissues always show an excess of free trypsin inhibitor and no evidence of active trypsin. The host protein is present inside the parasite, probably as the trypsin-inhibitor complex.
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