1976 年 80 巻 3 号 p. 649-652
A clottable protein (coagulogen) isolated from a hemocyte lysate of the Japanese horseshoe crab (Tachypleus tridentatus) was incubated with an endotoxin-activated clotting enzyme(s) partially purified from the same lysate, and its structural change during gel formation was examined. The results indicated that the enzymatic formation of gel involved limited proteolysis of the 46Arg-47Gly and 18Arg-19Thr linkages located in the N-terminal portion of the coagulogen, liberating peptide C.