牛玻璃酸酶酶学特性的研究

以牛睾丸为原料,对纯化后玻璃酸酶的酶学性质进行研究。结果表明,牛玻璃酸酶水解透明质酸钠的最适pH和温度分别为4.5、37℃,在4⁴5℃酶活稳定性较好。NaCl和BSA浓度分别为0.2、0.45mol/L时具有较高的酶活力。金属离子抑制该酶活力的顺序为,Fe3+>Mn2+>Zn2+>Al3+>Ca2+>K+>Mg2+。硫酸软骨素A浓度为1.2mg/mL时,酶活损失31.08%。硫酸软骨素B浓度为0.012mg/mL时,酶活增加1.36%。硫酸软骨素C浓度为1.2mg/mL时,酶活损失45.07%。肝素在0.012mg/mL时对酶存在抑制作用。人类血清蛋白在0.012mg/mL时可增加1.05%的酶活。半胱氨酸使酶失活。 

Study on enzymatic characteristics of hyaluronidase from bovine testicular

The enzyme used in this study was a partially purified sample of hyaluronidase, extracted and purified from bovine testicular. Using sodium hyaluronate as substrate, the pH optimum for the enzyme was pH4.5 and maximum activity was obtained at 37 ℃. The enzyme also required NaCl and BSA at a concentration of0.2mol/L and 0.45mol/L in the final incubation mixture for optimum activity. The hyaluronidase from bovine testicular was shown to be heat instable, and inhibited by metal ions, the inhibiting capacity was Fe3 +>Mn2 +>Zn2+>Al3+>Ca2+>K+>Mg2+. Chondroitin-sulphate A and C was inhibitor of bovine hyaluronidase, causing up to31.08% and 45.07% inhibition at 1.2mg/mL concentration. The enzyme activity was enhanced 1.36% and 1.05%by chondroitin-sulphate B and human serum protein at 0.012mg/mL concentration, respectively. Heparin inhibited enzyme activity at 0.012mg/mL concentration. Cysteine completely inhibited enzyme activity.