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Purification of human serum hyaluronidase using chromatofocusing

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  1. Separation of steroid isomers by ion mobility mass spectrometry

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A commercial chromatofocusing system was applied to Cohn's fraction III of human serum to purify hyaluronidase (E.C. The protein that eluted in the pH range 4.7-5.3 was pooled and precipitated by adding ammonium sulphate to 50% saturation. This sequence of fractionation purified hyaluronidase extensively by immunological criteria. It is shown that hyaluronidase is a population of enzymes displaying microheterogeneity. The commercial chromatofocusing system behaved as theoretically expected. The capacity of the gel is 3 mg per ml gel. Any overload will be trapped or precipitated in the gel. The gel is easy to handle and did not deteriorate on repeated use.
Original languageEnglish
JournalJournal of Chromatography A
Issue number1
Pages (from-to)173-9
Number of pages6
Publication statusPublished - 1982

    Research areas

  • Humans, Hyaluronoglucosaminidase, Immunoelectrophoresis, Isoelectric Focusing, Reference Values

ID: 32523458