Effect of Urea and Methylamine on Plasmin.

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Abstract
Active plasmin prepared from human plasma fraction III was freed of streptokinase by precipitation with 1[image] NaCl at pH 2. The product lost activity rapidly at 37[degree]C in neutral solutions. Urea or methylamine slowed this process to about the same degree that they inhibit digestion of casein by plasmin. The lability of plasmin therefore seems to be due to self-digestion. Agreement was demonstrated with the second order equation describing digestion of a rerersibly denatured enzyme by its active moiety. Autolysis at 37[degree] is very slow in 5 [image] methylamine and almost nil in 8 [image] urea. Solutions of plasmin in 0.0025 [image] HCl (pH 2.5) are stable for many days.

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