Matches in SemOpenAlex for { <https://semopenalex.org/work/W1506204176> ?p ?o ?g. }
Showing items 1 to 86 of
86
with 100 items per page.
- W1506204176 endingPage "1877" @default.
- W1506204176 startingPage "1871" @default.
- W1506204176 abstract "Hemolytically active, 125I-labeled delta-toxin from Clostridium perfringens was used to study the binding of this cytolysin to sheep, goat, human, rabbit, horse, mouse, and guinea pig erythrocytes. The extent of toxin binding was correlated with the known hemolytic specificity of the toxin. Detailed studies of the binding were carried out on sheep erythrocytes which showed the highest sensitivity to lysis by delta-toxin. Simultaneous determination of toxin binding and release of intracellular 86Rb+ and hemoglobin suggested that toxin binding and membrane damage were separate sequential events. Toxin binding was rapid (2-5 min) and temperature-dependent. The extent of binding was temperature-independent. Binding was saturable, specific, relatively tight (Ka = 4.4 X 10(8) M-1) and largely irreversible. A single type of binding site (7,000/sheep erythrocyte) was found. Cell-bound toxin was extractable by chaotropic ions. Preincubation of the toxin with N-acetylgalactosaminyl-[N-acetylneuraminyl]-galactosylglucosylceramide (GM2 ganglioside) inhibited both binding and hemolysis. Toxin binding was affected by pretreatment of sheep erythrocytes with pronase but not with trypsin or chymotrypsin. Cell treatment with neuraminidase prevented toxin binding by 30%. Preincubation of the toxin with specific immune sera blocked its binding on target cells. It is suggested that GM2 ganglioside, a more complex membrane component containing this glycolipid or a structurally related molecule is the binding site for delta-toxin on the surface of sensitive erythrocytes." @default.
- W1506204176 created "2016-06-24" @default.
- W1506204176 creator A5023156606 @default.
- W1506204176 creator A5034324350 @default.
- W1506204176 date "1983-02-01" @default.
- W1506204176 modified "2023-10-18" @default.
- W1506204176 title "Binding of Clostridium perfringens 125I-labeled delta-toxin to erythrocytes." @default.
- W1506204176 cites W1554825563 @default.
- W1506204176 cites W1580023435 @default.
- W1506204176 cites W1946446518 @default.
- W1506204176 cites W1966689948 @default.
- W1506204176 cites W1970195916 @default.
- W1506204176 cites W1973063119 @default.
- W1506204176 cites W1983649348 @default.
- W1506204176 cites W2004464696 @default.
- W1506204176 cites W2025616736 @default.
- W1506204176 cites W2026462493 @default.
- W1506204176 cites W2032088861 @default.
- W1506204176 cites W2035478701 @default.
- W1506204176 cites W2036913829 @default.
- W1506204176 cites W2037885552 @default.
- W1506204176 cites W2042044757 @default.
- W1506204176 cites W2050533461 @default.
- W1506204176 cites W2058601337 @default.
- W1506204176 cites W2064788768 @default.
- W1506204176 cites W2065533951 @default.
- W1506204176 cites W2067678324 @default.
- W1506204176 cites W2073879684 @default.
- W1506204176 cites W2075540274 @default.
- W1506204176 cites W2075907452 @default.
- W1506204176 cites W2090612967 @default.
- W1506204176 cites W2100837269 @default.
- W1506204176 cites W2115262231 @default.
- W1506204176 cites W2138042780 @default.
- W1506204176 cites W2168468281 @default.
- W1506204176 cites W2205918803 @default.
- W1506204176 cites W4238757920 @default.
- W1506204176 doi "https://doi.org/10.1016/s0021-9258(18)33069-2" @default.
- W1506204176 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6822539" @default.
- W1506204176 hasPublicationYear "1983" @default.
- W1506204176 type Work @default.
- W1506204176 sameAs 1506204176 @default.
- W1506204176 citedByCount "12" @default.
- W1506204176 countsByYear W15062041762013 @default.
- W1506204176 countsByYear W15062041762021 @default.
- W1506204176 crossrefType "journal-article" @default.
- W1506204176 hasAuthorship W1506204176A5023156606 @default.
- W1506204176 hasAuthorship W1506204176A5034324350 @default.
- W1506204176 hasBestOaLocation W15062041761 @default.
- W1506204176 hasConcept C185592680 @default.
- W1506204176 hasConcept C2777367657 @default.
- W1506204176 hasConcept C2779116991 @default.
- W1506204176 hasConcept C2781092032 @default.
- W1506204176 hasConcept C523546767 @default.
- W1506204176 hasConcept C54355233 @default.
- W1506204176 hasConcept C86803240 @default.
- W1506204176 hasConcept C89423630 @default.
- W1506204176 hasConceptScore W1506204176C185592680 @default.
- W1506204176 hasConceptScore W1506204176C2777367657 @default.
- W1506204176 hasConceptScore W1506204176C2779116991 @default.
- W1506204176 hasConceptScore W1506204176C2781092032 @default.
- W1506204176 hasConceptScore W1506204176C523546767 @default.
- W1506204176 hasConceptScore W1506204176C54355233 @default.
- W1506204176 hasConceptScore W1506204176C86803240 @default.
- W1506204176 hasConceptScore W1506204176C89423630 @default.
- W1506204176 hasIssue "3" @default.
- W1506204176 hasLocation W15062041761 @default.
- W1506204176 hasOpenAccess W1506204176 @default.
- W1506204176 hasPrimaryLocation W15062041761 @default.
- W1506204176 hasRelatedWork W1957943311 @default.
- W1506204176 hasRelatedWork W1969370843 @default.
- W1506204176 hasRelatedWork W1994948061 @default.
- W1506204176 hasRelatedWork W2089482209 @default.
- W1506204176 hasRelatedWork W2239534601 @default.
- W1506204176 hasRelatedWork W2800937934 @default.
- W1506204176 hasRelatedWork W3022148807 @default.
- W1506204176 hasRelatedWork W3098041677 @default.
- W1506204176 hasRelatedWork W4255257164 @default.
- W1506204176 hasRelatedWork W2187198178 @default.
- W1506204176 hasVolume "258" @default.
- W1506204176 isParatext "false" @default.
- W1506204176 isRetracted "false" @default.
- W1506204176 magId "1506204176" @default.
- W1506204176 workType "article" @default.