| pubmed-article:6275893 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6275893 | lifeskim:mentions | umls-concept:C1704353 | lld:lifeskim |
| pubmed-article:6275893 | lifeskim:mentions | umls-concept:C1412936 | lld:lifeskim |
| pubmed-article:6275893 | lifeskim:mentions | umls-concept:C0205390 | lld:lifeskim |
| pubmed-article:6275893 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
| pubmed-article:6275893 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:6275893 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:6275893 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6275893 | pubmed:dateCreated | 1982-4-22 | lld:pubmed |
| pubmed-article:6275893 | pubmed:abstractText | 1. Proenzymic C1r was purified from human plasma in a two-step technique involving indirect affinity chromatography on Sepharose Ig anti-C1s. The capacity of C1r to monomerize at pH 5.0 and to redimerize at neutral pH was used for selective elution of C1r. The yield in purified C1r was 39% from plasma; no trace of contaminating serine proteases was detected from [3H]diisopropyl phosphorofluoridate labelling of C1r. 2. C14 was able to undergo a two-way autoactivation: an intramolecular catalytic process catalysed by proenzymic C1r itself and an intermolecular reaction catalysed by activated C1r formed in the process of the reaction. DFP (5mM) and C1 Inh at a C1 Inh/C1r ratio of 1:1 were effective on the solely intermolecular activation, leading to partial inhibition of the autoactivation from proenzymic C1r: C1r formed during the activation was titrated by the inhibitors. Calcium, high ionic strength or acid pH decreased C1r activation. The pH effect was characterized by a slowed-down reaction below pH 6.0 and no net influence at values as high as 10.5. The two types of activation developed similarly as a function of pH. 3. Peripheral iodination of C1r revealed differences in label distribution between proenzymic (A chain moiety 48%, B chain moiety 52%) and activated C1r (A chain 20%, B chain 80%). Two different conformational states of C1r were also suggested by 125I-labelling at different temperatures. | lld:pubmed |
| pubmed-article:6275893 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6275893 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6275893 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6275893 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6275893 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6275893 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6275893 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6275893 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:6275893 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:6275893 | pubmed:author | pubmed-author:ColombM GMG | lld:pubmed |
| pubmed-article:6275893 | pubmed:author | pubmed-author:DuplaaA MAM | lld:pubmed |
| pubmed-article:6275893 | pubmed:author | pubmed-author:ArlaudG JGJ | lld:pubmed |
| pubmed-article:6275893 | pubmed:author | pubmed-author:VilliersC LCL | lld:pubmed |
| pubmed-article:6275893 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6275893 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:6275893 | pubmed:volume | 700 | lld:pubmed |
| pubmed-article:6275893 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6275893 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6275893 | pubmed:pagination | 118-26 | lld:pubmed |
| pubmed-article:6275893 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:6275893 | pubmed:meshHeading | pubmed-meshheading:6275893-... | lld:pubmed |
| pubmed-article:6275893 | pubmed:meshHeading | pubmed-meshheading:6275893-... | lld:pubmed |
| pubmed-article:6275893 | pubmed:meshHeading | pubmed-meshheading:6275893-... | lld:pubmed |
| pubmed-article:6275893 | pubmed:meshHeading | pubmed-meshheading:6275893-... | lld:pubmed |
| pubmed-article:6275893 | pubmed:year | 1982 | lld:pubmed |
| pubmed-article:6275893 | pubmed:articleTitle | Fluid phase activation of proenzymic C1r purified by affinity chromatography. | lld:pubmed |
| pubmed-article:6275893 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6275893 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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