Isolation and characterization of hyaluronidase from scorpion (Heterometrus fulvipes) venom.
Hyaluronidase (Hyaluronate lyase, E.C. 3.2.1.35) has been isolated from Heterometrus fulvipes scorpion venom by a combination of gel filtration on Sephadex G-75 and ion exchange chromatography on DEAE-cellulose. The enzyme preparation showed a single band on polyacrylamide gel electrophoresis and a molecular weight of 82,000. The final preparation was purified 27-fold. The optimum pH for enzyme activity was 4.0. No loss of activity was observed up to 30 degrees C and showed a sharp decrease in activity at 50 degrees C. Heparin inhibited the enzyme activity.
Ramanaiah
M
M
Department of Biochemistry, Sri Venkateswara University, Tirupati, India.
Parthasarathy
P R
PR
Venkaiah
B
B
D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006493:Heparin / Q000494:pharmacology; D006821:Hyaluronoglucosaminidase / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D012604:Scorpion Venoms / Q000032:analysis*; D013696:Temperature
D012604:Scorpion Venoms; D006493:Heparin; D006821:Hyaluronoglucosaminidase