Lysenin, a novel sphingomyelin-specific binding protein.

  title={Lysenin, a novel sphingomyelin-specific binding protein.},
  author={Akira Yamaji and Yoshiyuki Sekizawa and Kazuo Emoto and Hitoshi Sakuraba and Keizo Inoue and Hiromi Kobayashi and Masato Umeda},
  journal={The Journal of biological chemistry},
  volume={273 9},
Lysenin, a novel 41-kDa protein purified from coelomic fluid of the earthworm Eisenia foetida, induced erythrocyte lysis. Preincubation of lysenin with vesicles containing sphingomyelin inhibited lysenin-induced hemolysis completely, whereas vesicles containing phospholipids other than sphingomyelin showed no inhibitory activity, suggesting that lysenin bound specifically to sphingomyelin on erythrocyte membranes. The specific binding of lysenin to sphingomyelin was confirmed by enzyme-linked… CONTINUE READING
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