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PubMed1998

Inhibitors of pepsin, trypsin and chymotrypsin in seeds of plants consumed by humans and animals. I. Evaluation of pepsin, trypsin, and chymotrypsin inhibitors activity in seeds of 26 plant species.

Antipepsin, antitrypsin and antichymotrypsin activity was determined in seed extracts of 26 plants consumed by humans and animals (small bean, broad bean, pumpkin, kidney bean, charlock, pea, buckwheat, barley, maize, flax, lupine, poppy, almond, peanut, hazel, walnut, oat, millet, wheat, rice, rape, sunflower, lentils soya bean, vetch, rye). Antipepsin activity is found in the seeds of small bean, pumpkin, flax, peanut, walnut, oat, wheat, sunflower, lentils and soya bean. Antitrypsin and antichymotrypsin activities are of different intensity in seed extracts of all examined plants.

Animals↗
PubMed1982

Inhibition of free and bound trypsin-like enzymes.

1. The inhibition of beta-naphthylamidase activity of free trypsin, trypsin-Sepharose and a trypsin-like neutral protease on the surface of tumour cells have been studied in independent systems and with mixtures of free trypsin plus surface-bound trypsin. 2. Kinetic data have demonstrated that high-molecular-weight (protein) inhibitors of free trypsin are less effective inhibitors of trypsin-Sepharose and fail to inhibit the cell surface neutral protease. 3. Inhibition of mixtures of free trypsin plus trypsin-Sepharose follows independent kinetic plots for each component. The free trypsin is reacted before any Sepharose-bound trypsin reacts with high-molecular-weight inhibitors. 4. Low-molecular-weight inhibitors of trypsin also inhibit bound trypsin equally well. 5. Papain-derived peptides from high-molecular-weight inhibitors of trypsin inhibit free trypsin, trypsin-Sepharose and the cell-surface neutral protease almost equally well. 6. Fluorescence microscopy has shown that a high-molecular-weight inhibitor of trypsin does not bind to the tumour cell-surface neutral protease, but it does bind to trypsin-Sepharose. 7. The cell-surface neutral protease has been shown to be capable of activation of latent beta-naphthylamidase activity in the presence of excess extracellular inhibitors of free trypsin. 8. The mechanism by which trypsin-Sepharose remains partially active in the presence of excess inhibitor necessary to inhibit an equivalent quantity of free trypsin has been discussed. 9. These studies indicate that a search for inhibitors which are selectively active against the cell-surface neutral protease and have no action on trypsin-like enzymes in free solution must take into account the modifying effects of the cell surface on neutral protease activity.

Aminopeptidases↗