Purification of human serum hyaluronidase using chromatofocusing
Research output: Contribution to journal › Journal article › Research › peer-review
A commercial chromatofocusing system was applied to Cohn's fraction III of human serum to purify hyaluronidase (E.C.3.2.1.3.5). 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 language | English |
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Journal | Journal of Chromatography A |
Volume | 240 |
Issue number | 1 |
Pages (from-to) | 173-9 |
Number of pages | 6 |
ISSN | 0021-9673 |
Publication status | Published - 1982 |
ID: 34131416