Properties of a toxin from the sea anemone Stoichacis helianthus, including specific binding to sphingomyelin.
Properties of a toxin from the sea anemone Stoichacis helianthus, including specific binding to sphingomyelin.
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海葵 Stoichacis helianthus 毒素的特性,包括与鞘磷脂的特异性结合。
DOI:
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发表时间:
1976
影响因子:
11.1
通讯作者:
L. S. Avigad
中科院分区:
文献类型:
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作者:
A. W. Bernheimer;L. S. Avigad
Stoichactis helianthus toxin, a protein derived presumably from the nematocysts, was purified to homogeneity. It has a molecular weight of about 16,000, an isoelectric pH of 9.8, and it contains approximately 3.7% carbohydrate. It is powerfully hemolytic for erythrocytes derived from a variety of animal species, those of the cat being the most sensitive and those of the guinea pig the most resistant. The toxin is lytic also for rabbit blood platelets, and it destroys cultured fibroblasts but is inactive for several kinds of bacterial protoplasts and spheroplasts. The hemolytic activity is specifically inhibited by sphingomyelin, and it is proposed that this phospholipid is the constituent of the membrane which functions as receptor for the toxin. Supporting evidence includes the findings that enzymes known to destroy sphingomyelin (a) prevent erythrocyte membranes from inhibiting hemolysis, and (b) render erythrocytes resistant to lysis by the toxin. The mechanism underlying hemolysis may involve translocation of membrane sphingomyelin by virtue of a specific affinity of the coelenterate protein for this phospholipid.