pubmed-article:6903579 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6903579 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:6903579 | lifeskim:mentions | umls-concept:C0683598 | lld:lifeskim |
pubmed-article:6903579 | lifeskim:mentions | umls-concept:C0205345 | lld:lifeskim |
pubmed-article:6903579 | lifeskim:mentions | umls-concept:C1564378 | lld:lifeskim |
pubmed-article:6903579 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:6903579 | pubmed:dateCreated | 1981-1-29 | lld:pubmed |
pubmed-article:6903579 | pubmed:abstractText | The sera of some patients with SLE contain an IgG antibody (F-42) directed against the classical pathway C3 convertase (C-42), which is capable of stabilizing C42 in a dose-dependent manner. The half-life (T 1/2) of C42 is prolonged by F-42. In order to determine whether C4-binding protein was capable of reversing stabilization of C42, stabilized and unstabilized cell-bound C42 were exposed to purified C4-bp and the convertase activity was assessed. C4-bp was capable of accelerating the decay of C42 in a dose-dependent manner; 2 microgram/ml C4-bp reduced the T 1/2 of C42 from 5 to 2.5 min at 30 degrees C. On the other hand, 16 microgram C4-bp could reverse stabilization of C42 by F-42 from T 1/2 = 78 min to a T 1/2 - 40 min; 128 microgram C4-bp reduced the T 1/2 of stabilized C42 to 4 min. Functional inactivation of C42 occurs via enhanced decay-dissociation of C2 from the convertase by C4-bp, as shown by the release of 125I-C2i from the cell-bound convertase. Stabilization of C42 by F-42 is caused by prevention of decay-dissociation of 125I-C2. F-42 was also capable of stabilizing C4oxy2 even further, as shown by prolongation of the T 1/2 of cell-bound C4 oxy2 to a T 1/2 of at least 300 min at 30 degrees C. | lld:pubmed |
pubmed-article:6903579 | pubmed:language | eng | lld:pubmed |
pubmed-article:6903579 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6903579 | pubmed:citationSubset | AIM | lld:pubmed |
pubmed-article:6903579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6903579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6903579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6903579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6903579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6903579 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6903579 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6903579 | pubmed:month | Nov | lld:pubmed |
pubmed-article:6903579 | pubmed:issn | 0022-1767 | lld:pubmed |
pubmed-article:6903579 | pubmed:author | pubmed-author:GageA PAP | lld:pubmed |
pubmed-article:6903579 | pubmed:author | pubmed-author:van EsL ALA | lld:pubmed |
pubmed-article:6903579 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6903579 | pubmed:volume | 125 | lld:pubmed |
pubmed-article:6903579 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6903579 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6903579 | pubmed:pagination | 2051-4 | lld:pubmed |
pubmed-article:6903579 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
pubmed-article:6903579 | pubmed:meshHeading | pubmed-meshheading:6903579-... | lld:pubmed |
pubmed-article:6903579 | pubmed:meshHeading | pubmed-meshheading:6903579-... | lld:pubmed |
pubmed-article:6903579 | pubmed:meshHeading | pubmed-meshheading:6903579-... | lld:pubmed |
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pubmed-article:6903579 | pubmed:meshHeading | pubmed-meshheading:6903579-... | lld:pubmed |
pubmed-article:6903579 | pubmed:meshHeading | pubmed-meshheading:6903579-... | lld:pubmed |
pubmed-article:6903579 | pubmed:meshHeading | pubmed-meshheading:6903579-... | lld:pubmed |
pubmed-article:6903579 | pubmed:meshHeading | pubmed-meshheading:6903579-... | lld:pubmed |
pubmed-article:6903579 | pubmed:meshHeading | pubmed-meshheading:6903579-... | lld:pubmed |
pubmed-article:6903579 | pubmed:year | 1980 | lld:pubmed |
pubmed-article:6903579 | pubmed:articleTitle | Relative resistance of the F-42-stabilized classical pathway C3 convertase to inactivation by C4-binding protein. | lld:pubmed |
pubmed-article:6903579 | pubmed:publicationType | Journal Article | lld:pubmed |
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