Abstract
Dog trypsin (EC 3.4.4.4) was isolated from dog pancreatic juice on SP-Sephadex C-50. The preparation was homogeneous on disc electrophoresis at pH 4.3. On agarose gel electrophoresis at pH 8.6, dog pancreas trypsinogen had the mobility of an α 2- globulin and trypsin the mobility of a β-globulin. On gel filtration on Sephadex G-75 at pH 4.0, dog trypsin was eluted in the same fractions as bovine trypsin. It was inhibited by soybean trypsin inhibitor. Rabbit anti-dog trypsin inhibited the casein-olytic activity of bovine trypsin by about 60%.
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