Rapid purification of DesPro(2)-Val15-Leu17-aprotinin from the culture broth of a recombinant Saccharomyces cerevisiae |
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| Authors: | Barthel T Kula M R |
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| Affiliation: | Institut für Enzymtechnologie der Heinrich-Heine-Universit?t Düsseldorf, Forschungszentrum Jülich, Jülich, Postfach, Germany. |
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| Abstract: | A rapid two-step procedure has been developed for the purification of Despro(2)-Val15-Leu17-aprotinin from the culture supernatant of a recombinant yeast by affinity and ion-exchange chromatography. DesPro(2)-Val15-Leu17-aprotinin was purified to homogeneity, as demonstrated by dodecylsulfate gel electrophoresis and analysis of the N-terminal amino acid sequence. (c) 1993 John Wiley & Sons, Inc. |
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| Keywords: | affinity chromatography chymotrypsin Sepharose DesPro(2)-Val15-Leu17-aprotinin elastase inhibitor protease inhibitor |
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