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August 1964

Trypsin Release, Kinin Production, and ShockRelationship in Experimental and Human Pancreatitis

Arch Surg. 1964;89(2):322-331. doi:10.1001/archsurg.1964.01320020086014

As early as 1916 Peterson1 suggested that the fulminating nature of acute hemorrhagic pancreatitis was directly related to the digestion of plasma proteins by proteolytic enzymes. In 1950, Werle2 published his classic work on the hypotensive proteolytic material from the pancreas, kallikrein, and more recently, kallikrein was partially purified by Westerfield3 and Webster and Clark4 and shown to produce hypotension. Rocha e Silva,5,6 after demonstrating the ability of trypsin to release bound stores of histamine, discovered that trypsin also released from plasma α-2 globulins the hypotensive polypeptide bradykinin in much the same fashion as renin liberates the hypertensive polypeptide angiotensin. The object of the present investigation is to measure the liberation of proteolytic enzymes in pancreatitis and to relate this to the release of substances affecting vascular smooth muscle and capillary permeability.

Materials and Methods 

1. Experimental Pancreatitis.  —Healthy, adult mongrel dogs, ranging in weight

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