从石鱼（毒鲉）毒液中纯化透明质酸酶并进行部分特性分析。
Purification and partial characterization of hyaluronidase from stonefish (Synanceja horrida) venom.
作者信息
Poh C H, Yuen R, Chung M C, Khoo H E
机构信息
Department of Biochemistry, National University of Singapore, Kent Ridge.
出版信息
Comp Biochem Physiol B. 1992 Jan-Feb;101(1-2):159-63. doi: 10.1016/0305-0491(92)90172-n.
PMID:1499262
Abstract
- A marine hyaluronidase was purified 261-fold from the stonefish (Synanceja horrida) crude venom using Sephacryl S-200 HR and heparin affinity-gel chromatography. 2. Stonefish hyaluronidase has a pI of 9.2, a mol. wt of 62,000 and it was purified to a very high spec. act. of 1.6 x 10(6) NFU/mg protein. 3. It was heat sensitive and was inhibited by Cu2+, Hg2+ and heparin. 4. Stonefish hyaluronidase did not contain any haemorrhagic or lethal activity. 5. The N-terminal sequence of stonefish hyaluronidase has been determined to be A-P-S-X-D-E-G-N-K-K-A-D-N-L-L-V-K-K-I-N.
摘要
- 使用Sephacryl S - 200 HR和肝素亲和凝胶色谱法从石鱼（玫瑰毒鲉）粗毒液中纯化出一种海洋透明质酸酶，纯化倍数为261倍。2. 石鱼透明质酸酶的等电点为9.2，分子量为62,000，纯化至非常高的比活性，为1.6×10⁶ NFU/mg蛋白质。3. 它对热敏感，且受Cu²⁺、Hg²⁺和肝素抑制。4. 石鱼透明质酸酶不具有任何出血或致死活性。5. 石鱼透明质酸酶的N端序列已确定为A - P - S - X - D - E - G - N - K - K - A - D - N - L - L - V - K - K - I - N。
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