Abstract
Cell-free coelomic fluid obtained from the sea star Asterias forbesi rapidly neutralized, in a dose-dependent fashion, trypsin derived from several different animal species. Approximately 50 to 300 µg of bovine trypsin was inhibited per mg oftotal sea star coelomic fluid protein. Crude preparations of sea star and sea urchin trypsins isolated from gastric tissue, as well as purified human plasmin, were also neutralized upon addition to echinoderm coelomic fluid. In contrast, bovine α1-chymotrypsin and thrombin were not inactivated by the coelomic fluid inhibitor. The trypsin inhibitor was only mildly sensitive to heat or acid treatments and exhibited a molecular weight of ∼6500. The protease inactivator was also detected in cell lysates derived from washed coelomocytes collected in N-ethyl maleimide, as well as in cell-free coelomic fluid collected by non-surgical means.
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