ISSN:
1612-1112
Keywords:
Column liquid chromatography
;
Hydrophobic interaction chromatography
;
125I-labelled aprotinin
;
Serine proteinases
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary A previously described method for determining more than one serine proteinase simultaneously by hydrophobic interaction chromatography of their complexes with aprotinin is inapplicable when other UV-absorbing species are co-eluted. The suitability of125I-labelled aprotinin has therefore been tested as a reagent in the analysis of mixtures containing trypsin, α-chymotrypsin and kallikrein taken as models, in the presence of ribonuclease and lysozyme. A new procedure is described which, without introducing changes in the chromatographic separation, allows direct determination of serine proteinases in terms of molarity. Results obtained in experiments with solutions containing from 0.20 to 30.00 nmol of each serine proteinase are reported.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02275781
Permalink
