TY - JOUR

T1 - Purification of human serum hyaluronidase using chromatofocusing

AU - Fenger, M

PY - 1982

Y1 - 1982

N2 - 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.

AB - 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.

M3 - Journal article

VL - 240

SP - 173

EP - 179

JO - Journal of Chromatography

JF - Journal of Chromatography

SN - 0301-4770

IS - 1

ER -