Purification and partial characterization of hyaluronidase from stonefish (Synanceja horrida) venom

Comp Biochem Physiol B. 1992 Jan-Feb;101(1-2):159-63. doi: 10.1016/0305-0491(92)90172-n.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Electrophoresis, Polyacrylamide Gel
  • Fish Venoms / enzymology*
  • Glycoproteins / metabolism
  • Hyaluronoglucosaminidase / chemistry
  • Hyaluronoglucosaminidase / isolation & purification
  • Hyaluronoglucosaminidase / metabolism*
  • Hyaluronoglucosaminidase / toxicity
  • Hydrogen-Ion Concentration
  • Mice
  • Molecular Sequence Data
  • Molecular Weight
  • Temperature

Substances

  • Amino Acids
  • Fish Venoms
  • Glycoproteins
  • Hyaluronoglucosaminidase