PURIFICATION AND PARTIAL CHARACTERIZATION OF HYALURONIDASE FROM STONEFISH (SYNANCEJA-HORRIDA) VENOM

被引：65

作者：

POH, CH ^{[1
]}

YUEN, R ^{[1
]}

CHUNG, MCM ^{[1
]}

KHOO, HE ^{[1
]}

机构：

[1] NATL UNIV SINGAPORE, DEPT BIOCHEM, KENT RIDGE, SINGAPORE 0511, SINGAPORE

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1992年 / 101卷 / 1-2期

关键词：

D O I：

10.1016/0305-0491(92)90172-N

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：159 / 163

页数：5

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