ISSN:
1612-1112
Keywords:
Column liquid chromatography
;
Bovine trypsin
;
Porcine kallikrein
;
Bovine pancreatic trypsin inhibitor
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary The possibility of determining more than one enzyme at the same time has been examined. A new approach, based on the measurement of a direct and specific chromatographic signal obtained by hydrophobic interaction chromatography (HIC) of the stable complex formed with the inhibitor aprotinin, is proposed. A basic procedure for the quantitative determination of trypsin and kallikrein, taken as models, is described. The method is precise with a mean coefficient of variation of 3.1% and 3.5% for trypsin and kallikrein, respectively; the limit of determination for both enzymes is 0.17 nmol ml−1 in the original sample.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02278589
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