Abstract
The purification of a protease from pea seeds (about 350-fold) is described and some properties of the purified enzyme for which the name arvensin is proposed are discussed. The enzyme acts optimally on casein at pH 8.0; it is inhibited by some salts of heavy metals, but do not by iodoacetamide. It somewhat resembles trypsin. The specific activity of the most pure preparation is about a quarter of that of crystalline trypsin.
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