Archives of Surgery · 1964 · 59 citations · 12 references
Life SciencesBiochemistryVeterinary PhysiologyEnzymologyHemostasisProtein BiochemistryPlasma ProteinsProtein DegradationProteolytic EnzymesProteolytic ProcessingDigestive ProteasesKallikrein-kinin SystemProteolytic Enzyme ActivityProteolytic PathwaysVascular Smooth Muscle Regulation
As early as 1916 Peterson 1 suggested that the fulminating nature of acute hemorrhagic pancreatitis was directly related to the digestion of plasma proteins by proteolytic enzymes. In 1950, Werle 2 published his classic work on the hypotensive proteolytic material from the pancreas, kallikrein, and more recently, kallikrein was partially purified by Westerfield 3 and Webster and Clark 4 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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PROTEIN BINDING OF PANCREATIC PROTEOLYTIC ENZYMES*
Bernard J. Haverback, Barbara J. Dyce, Hallie F. Bundy et al. · Journal of Clinical Investigation · 1962 · 184 citations · Full text
Trypsin Inhibitors of Human Serum
Hallie F. Bundy, John W. Mehl · Journal of Biological Chemistry · 1959 · 126 citations · Full text