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Microbial hyaluronidase (EC 4.2.2.1) was isolated from the culture fluid of Staphylococcus aureus 0-15 with purification by precipitation with 1 volume of ethyl alcohol, chromatography on DEAE cellulose and ultrafiltration through DA type membranes with the pore size of 0.65 micron ("Millipore") and PM-10 membranes ("Amicon"). The specific activity of the enzyme averaged to 2700 turbidimetric units or 32130 IU. 6585-fold purification of the enzyme was performed. The optimum action on hyaluronic acid was observed at pH 5.0-6.5. Hyaluronidase was inhibited by Fe3+, Fe2+ and Cu2+, activated by Ca2+ and stabilized by 0.15 M NaCl. It was detected that the enzyme had two molecular forms with the isoelectric points of 5.4 and 6.5 and the molecular weights of 55 000 and 24 0000 D respectively. The glycoprotein nature of the enzyme was shown. The immobilized form of hyaluronidase on activated polyglucin, a soluble biocompatible polymer was prepared. The form is characterized by higher thermostability.
G I Kvesitadze, and
G L Broladze, and
Iu S Mikanadze, and
Ts S Turmanidze, and
T G Chanishvili
February 1965,
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G I Kvesitadze, and
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T G Chanishvili
December 1949,
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G I Kvesitadze, and
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T G Chanishvili
November 1968,
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G I Kvesitadze, and
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G I Kvesitadze, and
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G I Kvesitadze, and
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G I Kvesitadze, and
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G I Kvesitadze, and
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G I Kvesitadze, and
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February 1985,
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G I Kvesitadze, and
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Ts S Turmanidze, and
T G Chanishvili
January 1971,
European journal of biochemistry,
