Laboratory study demonstrates enzymatic behavior during prolonged autolysis in pancreatic extract, indicating whether trypsin undergoes destructive self-digestion.
Recently, Northrop and Kunitz (1) reported the isolation of a crystalline protein from beef pancreas, with constant tryptic and chemical properties, which they contend is identical with the enzyme trypsin.These authors find that crystalline trypsin, besides having the proteolytic powers to be expected, has slight milk-clotting powers which they believe are due to a contamination with a special milk-clotting enzyme of the pancreas.In 1907, Abderhalden and Pym (2) found that if liver is autolyzed long enough, the filtrates fail to give a biuret test.Because of this we were interested in determining whether pancreatic tissue could be similarly autolyzed until the biuret test was negative and, if so, whether it would still possess enzyme activity, or whether the trypsin would digest itself and thus become inactive.
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Kleiner et al. (1934) studied this question.
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