Comparison of metridiolysin from the sea anemone with thiol-activated cytolysins from bacteria
| Autor: | Kwang-Shin Kim, Lois S. Avigad, Alan W. Bernheimer |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
Erythrocytes
Bacterial Toxins Sea anemone Toxicology Dithiothreitol law.invention Hemolysin Proteins chemistry.chemical_compound Cnidarian Venoms law Animals Freeze Fracturing Metridium biology Erythrocyte Membrane Sulfhydryl Reagents Proteins biology.organism_classification Cytolysis Sea Anemones Membrane chemistry Biochemistry Streptolysins Streptolysin Electron microscope Bacteria |
| Zdroj: | Toxicon. 17:69-75 |
| ISSN: | 0041-0101 |
| Popis: | Metridiolysin, a cytotoxic protein from the sea anemone, Metridium senile , is activated by dithiothreitol and appears to be dependent for its activity on SH-groups. In this respect it resembles a class of SH-activated cytolytic bacterial proteins of which streptolysin O is the prototype. It shares also with SH-activated bacterial cytotoxins the capacity to produce ∼ 33 nm rings demonstrable by electron microscopic examination of negatively stained preparations of membranes from metridiolysin-lysed erythrocytes. Ring formation appears to correlate with alterations in membrane structure revealed by freeze-fracture electron microscopy. Further comparison of metridiolysin with the SH-activated bacterial cytotoxins reveals that both are inhibitable by low concentrations of cholesterol and that both have biological effects that are broadly similar. They differ, however, in certain other respects including molecular weight and capacity to dissociate into subunits. |
| Databáze: | OpenAIRE |
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