| pubmed-article:3922352 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3922352 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:3922352 | lifeskim:mentions | umls-concept:C0009498 | lld:lifeskim |
| pubmed-article:3922352 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:3922352 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:3922352 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:3922352 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:3922352 | lifeskim:mentions | umls-concept:C0439858 | lld:lifeskim |
| pubmed-article:3922352 | lifeskim:mentions | umls-concept:C0443177 | lld:lifeskim |
| pubmed-article:3922352 | lifeskim:mentions | umls-concept:C0348080 | lld:lifeskim |
| pubmed-article:3922352 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3922352 | pubmed:dateCreated | 1985-5-24 | lld:pubmed |
| pubmed-article:3922352 | pubmed:abstractText | Soluble classical-pathway C3 convertase and proconvertase were prepared from purified C4b-C2ox complex in the presence of Ni2+; the two complexes, stable for at least 15 h at 4 degrees C, were isolated by sucrose-density-gradient ultracentrifugation. The C3 convertase alone was able to cleave C3, and its decay was accelerated in the presence of C4-binding protein. The individual roles of Ni2+ and I2 treatment of C2 in the stabilization of the complexes seemed to be different and additive. 63Ni2+ binding coupled to h.p.l.c. analysis showed that 63Ni2+ bound only to the C2ox proteolytic fragment a (1 mol/mol) with a Kd of 26 microM. Competition studies between Ni2+ and Mg2+ indicated that only half of the Ni2+ bound to the C3 convertase was removed by Mg2+, whereas, in the same conditions, Ni2+ bound to C2ox proteolytic fragment a was not displaced, suggesting the presence of two sets of sites on the convertase. EDTA prevented the formation of both C3 convertase and proconvertase; EDTA had no effect on the preformed C3 convertase, whereas it dissociated the preformed proconvertase. | lld:pubmed |
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| pubmed-article:3922352 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3922352 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3922352 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3922352 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3922352 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:3922352 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3922352 | pubmed:author | pubmed-author:ColombM GMG | lld:pubmed |
| pubmed-article:3922352 | pubmed:author | pubmed-author:VilliersM BMB | lld:pubmed |
| pubmed-article:3922352 | pubmed:author | pubmed-author:ThielensN MNM | lld:pubmed |
| pubmed-article:3922352 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3922352 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:3922352 | pubmed:volume | 226 | lld:pubmed |
| pubmed-article:3922352 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3922352 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3922352 | pubmed:pagination | 429-36 | lld:pubmed |
| pubmed-article:3922352 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3922352 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:3922352 | pubmed:articleTitle | Soluble C3 proconvertase and convertase of the classical pathway of human complement. Conditions of stabilization in vitro. | lld:pubmed |
| pubmed-article:3922352 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3922352 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3922352 | lld:pubmed |
