Mechanism of activation by CA2+ of hemolysis induced by lytic polypeptide equinatoxin II
eKhNUIR
Переглянути архів Інформація| Поле | Співвідношення | |
| Title |
Mechanism of activation by CA2+ of hemolysis induced by lytic polypeptide equinatoxin II
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| Creator |
Rudenko, S.V.
Shchetinina, E.M. |
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| Subject |
erythrocyte
hemolysis divalent cations equinatoxin II |
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| Description |
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.
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| Date |
2012-12-04T00:42:22Z
2012-12-04T00:42:22Z 2011 |
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| Type |
Article
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| Identifier |
Журнал
http://dspace.univer.kharkov.ua/handle/123456789/7235 |
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| Language |
en
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| Relation |
Биофизический вестник;26(1)
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| Publisher |
Харьковский Национальный Университет им. В.Н.Каразина
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