| Autor: |
Bansal, M. R., Kanwar, K. C., Gupta, G. S. |
| Zdroj: |
Reproduction; March 1982, Vol. 64 Issue: 2 p267-273, 7p |
| Abstrakt: |
Summary.Hyaluronidase from rhesus monkey testes was purified by detergent extraction, ammonium sulphate fractionation, Sephadex G-200 column chromatography and concanavalin A—Sepharose affinity chromatography. The purified hyaluronidase showed one protein band on acrylamide gel electrophoresis. Antibodies to the purified hyaluronidase were raised in rabbits and showed a single precipitin line by Ouchterlony gel diffusion. The enzyme had a molecular weight of 62 000. The Kmwas 0·5 mg/ml for hydrolysis of hyaluronic acid at 37°C. The optimum pH for the enzyme was 5·0 but activity was present over a broad pH range. The hyaluronidase was inhibited by HgCl2, CuSO4, FeSO4and p-chloromercuribenzoate all at a concentration of 2 × 10−4m. Cysteine protected the enzyme against HgCl2inhibition. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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