Purification and partial characterization of hyaluronidase from stonefish (Synanceja horrida) venom.
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.
Poh
C H
CH
Department of Biochemistry, National University of Singapore, Kent Ridge.
Yuen
R
R
Chung
M C
MC
Khoo
H E
HE
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005397:Fish Venoms / Q000201:enzymology*; D006023:Glycoproteins / Q000378:metabolism; D006821:Hyaluronoglucosaminidase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism* / Q000633:toxicity; D006863:Hydrogen-Ion Concentration; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013696:Temperature
D000596:Amino Acids; D005397:Fish Venoms; D006023:Glycoproteins; D006821:Hyaluronoglucosaminidase