pubmed-article:3711989 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3711989 | lifeskim:mentions | umls-concept:C0027819 | lld:lifeskim |
pubmed-article:3711989 | lifeskim:mentions | umls-concept:C0039617 | lld:lifeskim |
pubmed-article:3711989 | lifeskim:mentions | umls-concept:C0682527 | lld:lifeskim |
pubmed-article:3711989 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:3711989 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:3711989 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:3711989 | pubmed:dateCreated | 1986-7-1 | lld:pubmed |
pubmed-article:3711989 | pubmed:abstractText | Tetanus toxin is known to bind neuronal tissue selectively. To study the interactions of this potent neurotoxin in an intact cell system, the binding of 125I-tetanus toxin was characterized in a neuroblastoma retina hybrid cell line, N18-RE-105. The binding of 125I-tetanus toxin to membranes prepared from N18-RE-105 cells showed many similarities to the interactions of 125I-toxin with rat synaptic membranes. The binding was decreased with increasing temperature, ionic strength, and pH. 125I-Toxin bound to membranes with high affinity: KD = 0.62 +/- 0.05 nM; Bmax = 196 +/- 45 pmol/mg protein. Quantitative thin-layer chromatography and acid-degradation analysis revealed that N18-RE-105 cells contained polysialogangliosides GD1a and GT1b in high concentrations. An assay was developed to quantitate surface-bound and internalized 125I-tetanus toxin by exploiting the observation that surface-bound 125I-toxin is susceptible to pronase digestion. When cells were incubated with 125I-tetanus toxin at 0 degree C, all of the bound 125I-toxin could be degraded with pronase. In contrast, when the incubations were performed at 37 degrees C, within 10 min about 50% of the total cell-associated 125I-toxin was pronase-resistant. Temperature pulse experiments demonstrated that 125I-tetanus toxin that was bound to cells at 0 degree C rapidly disappeared from the surface when the cells were warmed to 37 degrees C, as revealed by the appearance of pronase-resistant radioactivity. This internalization was sensitive to metabolic inhibitors.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
pubmed-article:3711989 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:language | eng | lld:pubmed |
pubmed-article:3711989 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3711989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3711989 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3711989 | pubmed:month | May | lld:pubmed |
pubmed-article:3711989 | pubmed:issn | 0270-6474 | lld:pubmed |
pubmed-article:3711989 | pubmed:author | pubmed-author:SchnaarR LRL | lld:pubmed |
pubmed-article:3711989 | pubmed:author | pubmed-author:SandbergKK | lld:pubmed |
pubmed-article:3711989 | pubmed:author | pubmed-author:RogersT BTB | lld:pubmed |
pubmed-article:3711989 | pubmed:author | pubmed-author:NicholsTT | lld:pubmed |
pubmed-article:3711989 | pubmed:author | pubmed-author:WaltonK MKM | lld:pubmed |
pubmed-article:3711989 | pubmed:author | pubmed-author:StaubG CGC | lld:pubmed |
pubmed-article:3711989 | pubmed:author | pubmed-author:BaichwalRR | lld:pubmed |
pubmed-article:3711989 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3711989 | pubmed:volume | 6 | lld:pubmed |
pubmed-article:3711989 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3711989 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3711989 | pubmed:pagination | 1443-51 | lld:pubmed |
pubmed-article:3711989 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:3711989 | pubmed:year | 1986 | lld:pubmed |
pubmed-article:3711989 | pubmed:articleTitle | Characterization of the binding and internalization of tetanus toxin in a neuroblastoma hybrid cell line. | lld:pubmed |
pubmed-article:3711989 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3711989 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:3711989 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:3711989 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3711989 | lld:pubmed |