pubmed-article:4062888 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:4062888 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:4062888 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:4062888 | lifeskim:mentions | umls-concept:C0068655 | lld:lifeskim |
pubmed-article:4062888 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
pubmed-article:4062888 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:4062888 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
pubmed-article:4062888 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:4062888 | pubmed:dateCreated | 1985-12-4 | lld:pubmed |
pubmed-article:4062888 | pubmed:abstractText | The proteins from labelled human spleen membranes and polymorphonuclear leucocytes which bind to the iC3b fragment of complement component C3 were prepared by iC3b-Sepharose chromatography in the presence of bivalent cations. Complement receptor type 3(CR3) was eluted from iC3b-Sepharose by removal of bivalent cations. Complement receptors type 1 and 2 (present in spleen but not in polymorphonuclear leucocytes) were sequentially eluted by an NaCl gradient. An additional protein of Mr 135 000 was eluted from iC3b-Sepharose under the same conditions as those used to elute CR3. Preabsorption of the starting material on an anti-(CR3 beta-subunit) antibody column before iC3b-Sepharose chromatography removed the alpha- and beta-chains of CR3 and the 135 000-Mr protein. Preabsorption with iC3b-Sepharose before the anti-(CR3 beta-subunit) antibody column showed that iC3b binds CR3 and p150,95, the smallest member of the group of three homologous proteins that share the same beta-subunit. | lld:pubmed |
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pubmed-article:4062888 | pubmed:language | eng | lld:pubmed |
pubmed-article:4062888 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:4062888 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:4062888 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:4062888 | pubmed:month | Oct | lld:pubmed |
pubmed-article:4062888 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:4062888 | pubmed:author | pubmed-author:SimR BRB | lld:pubmed |
pubmed-article:4062888 | pubmed:author | pubmed-author:MicklemK JKJ | lld:pubmed |
pubmed-article:4062888 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:4062888 | pubmed:day | 1 | lld:pubmed |
pubmed-article:4062888 | pubmed:volume | 231 | lld:pubmed |
pubmed-article:4062888 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:4062888 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:4062888 | pubmed:pagination | 233-6 | lld:pubmed |
pubmed-article:4062888 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:4062888 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:4062888 | pubmed:articleTitle | Isolation of complement-fragment-iC3b-binding proteins by affinity chromatography. The identification of p150,95 as an iC3b-binding protein. | lld:pubmed |
pubmed-article:4062888 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:4062888 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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