Hyaluronidase is an enzyme that catalyzes the hydrolysis of hyaluronic acid (1). Hyaluronidase isolated in mammalian testis has been used in medicine in conjunction with local anesthetic to speed its dispersion (2-3). There are many animal-derived clinical grade hyaluronidases available but all have potential BSE problem. Only one recombinant hyaluronidase was approved in 2005 by US FDA.In this study, we have established the high yield purification process for natural hyaluronidase from Korean bovine testis. Solubilizing bovine testis with detergent containing buffer, supernatant was treated with ammonium sulfate and acid. Precipitates were then further purified by ion-exchange chromatography. About 120,000 units of hyaluronidase were collected from 200 g of bovine testis. The activity of isolated hyaluronidase was determined by the test method in USP-NF and 56 kDa protein was identified as bovine hyaluronidase by Western blot analysis. Isolated natural hyaluronidase from bovine testis has been compared with recombinant bovine hyaluronidase in E. coli. The recombinant bovine hyaluronidase will be used for a safe biopharmaceutical once its safety and efficacy are confirmed.
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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