Ramanaiah M, Parthasarathy P R, Venkaiah B
Department of Biochemistry, Sri Venkateswara University, Tirupati, India.
Biochem Int. 1990;20(2):301-10.
Hyaluronidase (Hyaluronate lyase, E.C. 3.2.1.35) has been isolated from Heterometrus fulvipes scorpion venom by a combination of gel filtration on Sephadex G-75 and ion exchange chromatography on DEAE-cellulose. The enzyme preparation showed a single band on polyacrylamide gel electrophoresis and a molecular weight of 82,000. The final preparation was purified 27-fold. The optimum pH for enzyme activity was 4.0. No loss of activity was observed up to 30 degrees C and showed a sharp decrease in activity at 50 degrees C. Heparin inhibited the enzyme activity.
透明质酸酶（透明质酸裂合酶，E.C. 3.2.1.35）已通过在Sephadex G - 75上进行凝胶过滤和在DEAE - 纤维素上进行离子交换色谱相结合的方法，从黄肥尾蝎毒液中分离出来。该酶制剂在聚丙烯酰胺凝胶电泳上显示出单一谱带，分子量为82,000。最终制剂纯化了27倍。酶活性的最适pH为4.0。在30℃以下未观察到活性丧失，而在50℃时活性急剧下降。肝素抑制该酶的活性。
