Preparative Purification of Dipeptidyl Peptidase IV |
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| Authors: | Roland Seidl Wolfram Schaefer |
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| Institution: | Max-Planck-Institute for Biochemistry , Am Klopferspitz 18aD-8033, Martinsried |
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| Abstract: | Abstract Dipeptidyl-Peptidase IV was purified from pig kidney by ammonium sulfate fractionation, gel filtration, QAE-cellulose chromatography and affinity columns with Gly-Pro- and Concanavalin A-Sepharose. The specific activity of the purified enzyme is 41.8 units/mg. Polyacrylamide gel electrophoresis and silver staining show a single band. The enzyme preparation is free of aminopeptidase and dipeptidase activity, proved fluorimetrically and by gas chromatography/mass spectrometry. The most important procedure for removal of contaminating enzyme activities is a stepwise NaCl-gradient on a QAE-ZetaPrep ion exchange disk. |
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