Mechanism of activation by CA2+ of hemolysis induced by lytic polypeptide equinatoxin II
| dc.contributor.author | Rudenko, S.V. | |
| dc.contributor.author | Shchetinina, E.M. | |
| dc.date.accessioned | 2012-12-04T00:42:22Z | |
| dc.date.available | 2012-12-04T00:42:22Z | |
| dc.date.issued | 2011 | |
| dc.description.abstract | Equinatoxin II is a cytolytic polypeptide from the sea anemone Actinia equina L. which forms pores in natural and artificial membranes. In the present study, we show that the mechanism by which Ca2+ activates toxin-induced hemolysis of human red blood cells consists of the ability of Ca2+ which enters the cell presumably through preformed toxin-induced pores and acts inside the cell to increase the rate of toxin binding to the membrane. As a result, a larger amount of pores is produced thus increasing the rate of hemolysis. In addition, the data reveal that equinatoxin II induces hemolysis of RBC interacting with a limited number of toxin-binding sites (receptors) with an upper estimate of (180 35) 103 sites per one cell. The total number of toxin-binding sites does not depend on the presence of Ca2+. These data strongly suggest that specific receptor must exist on the erythrocyte membrane to mediate the hemolytic action of this toxin. | en |
| dc.identifier.citation | Журнал | en |
| dc.identifier.uri | https://ekhnuir.karazin.ua/handle/123456789/7235 | |
| dc.language.iso | en | en |
| dc.publisher | Харьковский Национальный Университет им. В.Н.Каразина | en |
| dc.relation.ispartofseries | Биофизический вестник;26(1) | |
| dc.subject | erythrocyte | en |
| dc.subject | hemolysis | en |
| dc.subject | divalent cations | en |
| dc.subject | equinatoxin II | en |
| dc.title | Mechanism of activation by CA2+ of hemolysis induced by lytic polypeptide equinatoxin II | en |
| dc.type | Article | en |
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