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  • 1
    Electronic Resource
    Electronic Resource
    Purification of125I-labelled aprotinin by hydrophobic interaction chromatography (1993)
    Springer
    Chromatographia 35 (1993), S. 93-96 
    Details
    ISSN: 1612-1112
    Keywords: Liquid chromatography ; Bovine pancreatic trypsin inhibitor ; 125I-labelled compounds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary 125I-aprotinin has been prepared and purified by affinity chromatography in combination with hydrophobic interaction chromatography (HIC). The method allows the preparation of the labelled inhibitor practically carrier-free, in saline solution without organic modifier and the isolated compound retained inhibition activity. Recovery of radioactive material was virtually quantitative, without substantial accumulation of radioactivity on the column. Compared with currently used procedures, the method is more reliable because the labelled polypeptide is collected by following its specific chromatographic signal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02278563
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  • 2
    Electronic Resource
    Electronic Resource
    Simultaneous determination of two serine proteinases by hydrophobic interaction chromatography (1993)
    Springer
    Chromatographia 35 (1993), S. 381-386 
    Details
    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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  • 3
    Electronic Resource
    Electronic Resource
    RP-HPLC as an evaluation method for the behaviour of urinary trypsin inhibitors (1988)
    Springer
    Chromatographia 26 (1988), S. 369-371 
    Details
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; Urinary trypsin inhibitors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Human urine contains a family of trypsin inhibitors. Procedures for their purification and characterization involve laborious techniques and the conclusions are different in the identification of the separated compounds. We report results obtained by applying our RP-HPLC method to some procedures adopted by different authors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02268183
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  • 4
    Electronic Resource
    Electronic Resource
    125I-labelled aprotinin as reagent for simultaneous determination of serine proteinases by hydrophobic interaction chromatography (1993)
    Springer
    Chromatographia 37 (1993), S. 471-474 
    Details
    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
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  • 5
    Electronic Resource
    Electronic Resource
    p-Hydroxymercuribenzoate as thiol-protein modifier for simultaneous determination of glycolytic enzymes by hydrophobic-interaction chromatography (1999)
    Springer
    Chromatographia 49 (1999), S. 47-53 
    Details
    ISSN: 1612-1112
    Keywords: Column liquid chromatography ; Glycolytic enzymes ; p-Hydroxymercuribenzoate ; 203Hg-labelledp-hydroxymercuribenzoate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The use of hydrophobic-interaction chromatography (HIC) is proposed for the simultaneous determination of more than one thiol-protein after formation of the corresponding mercury mercaptides withp-hydroxymercuribenzoate (PHMB). The new chromatographic procedure, based on the HIC separation of the modified proteins from each other and from excess organomercury reagent has been successfully applied to the quantitative determination of phosphoglucose isomerase (PGI) and phosphoglucose mutase (PGM) in crude PGI powder, and of L-lactate dehydrogenase, PGM and aldolase in crude pyruvate kinase from rabbit muscle. The suitability of203Hg-labelled PHMB has been tested in the analysis of mixtures, which give barely distinguishable UV-peaks owing to the presence of other non-thiol components in the sample. For this purpose glyceraldehyde 3-phosphate dehydrogenase (GAPDHy) and PGIy from bakers yeast have been considered. Results obtained in experiments performed by both procedures are reported.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02467186
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