Abstract
1. Tryptase activity in serum (pH 7.8, hydrolysis of casein). is generally inhibited by serum itself and is not to be recognized directly.
2. The inhibitory action against pancreas trypsin can be demonstrated not only in albumin fraction but also in globulin fraction of serum.
3. The smaller the pH value (under pH 4.2) employed for the acid treatment is, the more evident is it that the antitryptic activity of serum after the treatment disappears in proportion to the degree of degeneration of serum protein. The appearance of serum tryptase activity is distinct after the treatment rather at more than pH 4.8.
4. After the adsorption with kaolin at nearly isoelectric point of a serum protein, antitryptic activity of serum disappears not proportionally to the decrease in N-amount of the serum.