Clinical Chemistry
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Clinical Chemistry 18: 1385-1394, 1972;
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Clinical Chemistry, Vol 18, 1385-1394, Copyright © 1972 by the American Association for Clinical Chemistry

Differentiation of Trypsin-Like Enzymes in Human Plasma

Herbert D. Gullick 1

1 Department of Surgery, State University of New York Upstate Medical Center; and the Veterans Administration Hospital, Syracuse, N. Y. 13210.

The arginine amidase and arginine esterase activity of human plasma is compared with that of trypsin, thrombin, plasmin, and kallikrein by using the homologous synthetic amino acid substrates, benzoyl arginine amide (BAA) and benzoyl arginine ethyl ester (BAEE). Hydrolyses of BAA and BAEE in plasma are distinguished by several features: pH optimum, heat stability, storage stability, effect of dilution, surface contact activation, streptokinase activation, inhibition by proteolytic enzyme inhibitor, and range of normal variation. The differential sensitivity of trypsin, thrombin, plasmin, and kallikrein toward these substrates and the similarity in reaction characteristics of plasma-BAA and trypsin-BAA provide evidence that the arginine amidase activity of plasma represents trypsin, while the arginine esterase activity of plasma is nonspecific.


Key Words: coagulation • pancreatitis • plasma kinins • kallikrein • streptokinase • benzoyl arginine amide and benzoyl arginine ethyl ester as substrates • amylase • esterase • lipase • plasmin • complement • thrombin • inhibitor in plasma • normal values

Submitted on April 6, 1972
Accepted on August 17, 1972




The following articles in journals at HighWire Press have cited this article:


Home page
 Annals of Clinical & Laboratory ScienceHome page
R. W. Gullick and F. W. Sunderman Jr.
Herbert D. Gullick, M.D. (1922-2000)
Ann. Clin. Lab. Sci., April 1, 2001; 31(2): 213 - 214.
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