Arginine Esterase Activity of the Contact (Hageman) Factor

Summary

It was found that alcaline eluates obtained from kaolin shaken with normal intact plasma accelerated the clotting time of Hageman or exhausted plasma and exhibited significant arginine esterase activity. Alcaline kaolin eluate obtained in the same manner from Hageman plasma was lacking in any significant clotting and arginine esterase activity.

Arginine esterase activity of the alcaline kaolin eluate was inhibited by soybean trypsin inhibitor (SBI) and pancreatic trypsin inhibitor (PI) and was completely destroyed after 1 hour incubation at 65° C. Optimal conditions for this activity were found at pH 7,5—8,0.

Arginine esterase activity of the alcaline kaolin eluates was not connected with the thrombin or plasmin contaminations. Purified preparations of a plasma thromboplastin were devoided of any significant arginine esterase activity.

It is concluded that arginine esterase activity contained in alcaline kaolin eluate is connected with the active Hageman factor or related to its activation by silica surfaces.

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