Comparative Biochemistry & Physiology B 69(3): 529-534
1981
Collagenase isolated from C. quinquecirrha (sea nettle) nematocyst venom was purified 237-fold using 3 sequential ion exchange chromatographic steps. Collagenase had optimal activity as physiological pH and temperature ranges. The enzyme was activated by Ca2+ and Na+ and reversibly inhibited by EDTA. The enzyme was not inhibited by phenylmethyl-sulfonyl fluoride but a number of chelating agents, Cys and many metal ions inhibited the collagenase.