Purification and partial characterization of hyaluronidase from stonefish (Synanceja horrida) venom. |
| |
| Authors: | C H Poh R Yuen M C Chung H E Khoo |
| |
| Affiliation: | Department of Biochemistry, National University of Singapore, Kent Ridge. |
| |
| Abstract: | 1. 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. |
| |
| Keywords: | |
|
|
