The Journal of Experimental Medicine
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The Journal of Experimental Medicine, Vol 95, 571-591, Copyright, 1952, by The Rockefeller Institute for Medical Research New York

ARTICLE

STUDIES ON THE INHIBITION OF PROTEOLYTIC ENZYMES BY SERUM : I. THE MECHANISM OF THE INHIBITION OF TRYPSIN, PLASMIN, AND CHYMOTRYPSIN BY SERUM USING FIBRIN TAGGED WITH I131 AS A SUBSTRATE



N. Raphael Shulman M.D.1

1 From the Sloan-Kettering Institute for Cancer Research, and the Department of Medicine, Memorial Hospital, New York

The mechanism of the inhibition of trypsin, plasmin, and chymotrypsin by serum was studied using fibrin tagged with radioactive iodine as a substrate.

Enzyme-inhibitor relationships were studied by: (a) varying the concentration of serum; (b) varying the concentration of enzyme; and (c) by diluting the enzyme-serum mixture. The results indicate that the inhibition of trypsin, plasmin, and chymotrypsin is a stoichiometric and irreversible reaction.

By using the Lineweaver-Burk graphical method of analysis it was demonstrated that the inhibition of trypsin and chymotrypsin is a non-competitive reaction. This finding supports the conclusion that inhibition by serum is an irreversible type of reaction.

The substrate was found to exert a retarding effect on the activity of plasmin. The possibility of a plasmin inhibitor in fibrinogen was suggested.

The suitability of the various procedures used in evaluating serum proteolytic inhibition was discussed.

 Submitted on March 10, 1952


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