[HTML][HTML] Lysenin, a novel sphingomyelin-specific binding protein
A Yamaji, Y Sekizawa, K Emoto, H Sakuraba… - Journal of Biological …, 1998 - ASBMB
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 immunosorbent assay, TLC …
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 immunosorbent assay, TLC …