Abstract
In our laboratory we have isolated to this date two forms of trypsin and three forms of chymotrypsin from homogenates of human pancreatic tissue [1-4]. However, we have been unable to detect the presence of any specific enzyme which hydrolyzes elastin. Nevertheless, a proteolytic enzyme (Protease E), which hydrolyses all of the conventional synthetic substrates used for identification of elastase activity (benzyloxycarbonyl-L-alanine p-nitrophenyl ester, N-tert-butyl-oxycarbonyl-L-alanine p-nitrophenyl ester and acetyl-L-alanyl-L-alanyl-L-alanine methyl ester) has been identified and purified to homogeneity. This enzyme is referred to elsewhere as a second proteolytic component isolated during the purification of anionic trypsin [2].
This research was supported in part by grants from the National Institute of Health and the Council for Tobacco Research, USA.
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References
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Mallory, P.A., Travis, J. (1974). Properties and Inhibition Spectrum of a New Human Pancreatic Protease. In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds) Proteinase Inhibitors. Bayer-Symposium, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87966-1_29
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DOI: https://doi.org/10.1007/978-3-642-87966-1_29
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