NDLI: Determination of trypsin, chymotrypsin and kallikrein in porcine pancreas extracts by capillary zone electrophoresis

Content Provider	Springer Nature Link
Author	Braca, F. Secco, F. Spinetti, M. Raspi, G.
Copyright Year	2002
Abstract	A new method for the direct detection of trypsin, chymotrypsin A and kallikrein from porcine pancreas by capillary zone electrophoresis is proposed. Optimum conditions for quantitative determination were investigated which also allow the unequivocal distinction of trypsin and chymotrypsin according to porcine or bovine source. For each enzyme good linearity and precision were obtained, with a detection limit of 5.0 μg mL−1. In addition, the formation of the complexes between trypsin and basic pancreatic trypsin inhibitor, as well as that between kallikrein and the same inhibitor, have been investigated. Such complexes can be clearly distinguished either from the unreacted enzyme or the excess inhibitor and their use for analytical purposes has been evidenced. The method is rapid and sensitive and has been applied to determine enzymes in several porcine pancreas extracts. The levels of the active compounds in various kinds of commercial preparations were easily determined with relative standard deviations ranging between 3.3 and 4.9%, and recoveries from 95.8% to 102.4%.
Starting Page	693
Ending Page	699
Page Count	7
File Format	PDF
ISSN	00095893
Journal	Chromatographia
Volume Number	55
Issue Number	11-12
e-ISSN	16121112
Language	English
Publisher	Vieweg Verlag
Publisher Date	2002-01-01
Publisher Place	Wiesbaden
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Capillary zone electrophoresis Hydrophobic interaction chromatography Pancreatic proteases Aprotinin Porcine pancreas extracts Analytical Chemistry Organic Chemistry Pharmacy Biochemistry Plant Sciences Measurement Science, Instrumentation
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Clinical Biochemistry

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