[Purification and properties of staphylococcal hyaluronidase].
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.
D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D004800:Enzymes, Immobilized; D006821:Hyaluronoglucosaminidase / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009391:Nephelometry and Turbidimetry; D013211:Staphylococcus aureus / Q000201:enzymology*; D013696:Temperature; D014462:Ultrafiltration
D004800:Enzymes, Immobilized; D006821:Hyaluronoglucosaminidase
Ochistka i svoĭstva stafilokokkovoĭ gialuronidazy.