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Comparison of proteolytic activities of the enzyme complex from mammalian pancreas and pancreatin

Comparison of proteolytic activities of the enzyme complex from mammalian pancreas and pancreatin The proteolytic activity and thermal stability of the enzyme complex of a cell suspension from pig and bovine pancreas glands was compared with those of pancreatin. The enzyme complex displayed the highest thermal stability and activity at 50°C. The kinetic constants, energies of activation and inactivation of the enzyme complex, and pH optimum (7.0 ± 0.1) at which this complex had the maximum proteolytic activity were determined. Pancreatin had a pH optimum of 8.0 ±0.1. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Comparison of proteolytic activities of the enzyme complex from mammalian pancreas and pancreatin

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References (5)

Publisher
Springer Journals
Copyright
Copyright © 2000 by Berdutina, Neklyudov, Ivankin, Karpo, Mitaleva
Subject
Life Sciences; Biochemistry, general; Microbiology; Medical Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1007/BF02738043
Publisher site
See Article on Publisher Site

Abstract

The proteolytic activity and thermal stability of the enzyme complex of a cell suspension from pig and bovine pancreas glands was compared with those of pancreatin. The enzyme complex displayed the highest thermal stability and activity at 50°C. The kinetic constants, energies of activation and inactivation of the enzyme complex, and pH optimum (7.0 ± 0.1) at which this complex had the maximum proteolytic activity were determined. Pancreatin had a pH optimum of 8.0 ±0.1.

Journal

Applied Biochemistry and MicrobiologySpringer Journals

Published: Oct 27, 2007

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