Abstract
The purification and characterization of a tumor-associated trypsin inhibition (TATI) was described previously. Studies on its N-terminal sequence suggested identity with the pancreatic secretory trypsin inhibitor (PSTI). The occurrence of a TATI-like activity in human seminal plasma was reported. Concentrations of this inhibitor in seminal plasma varied considerably (4-500 ng/ml, n = 50). In radioimmunoassay the dose-response curves of the new seminal plasma inhibitor and purified TATI were parallel. The similarity between these 2 inhibitors was demonstrated by gel filtration, reverse phase liquid chromatography and ion-exchange chromatography. By ion exchange chromatography the new inhibitor could be separated from the main seminal plasma trypsin inhibitors. Purified TATI inhibited human acrosin effectively.

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