| pubmed-article:9187240 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9187240 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:9187240 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
| pubmed-article:9187240 | lifeskim:mentions | umls-concept:C0022646 | lld:lifeskim |
| pubmed-article:9187240 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:9187240 | lifeskim:mentions | umls-concept:C0053358 | lld:lifeskim |
| pubmed-article:9187240 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
| pubmed-article:9187240 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:9187240 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9187240 | pubmed:dateCreated | 1997-7-1 | lld:pubmed |
| pubmed-article:9187240 | pubmed:abstractText | Outer renal medulla calmodulin-binding proteins from a soluble protein fraction and a plasma membrane fraction solubilized in CHAPS were retained on a calmodulin-Sepharose 4B column in the presence of Ca2+, and subsequently eluted by EGTA. The calmodulin-binding proteins constituted 2.5% of the soluble protein and 0.1% of the solubilized membrane protein. beta2-glycoprotein I was identified as a calmodulin-binding protein both by N-terminal sequencing and by immunoblotting. Quantification showed that beta2-glycoprotein I constituted the major part (approx. 35%) of the calmodulin-binding membrane proteins, but only a minor part (approx. 0.1%) of the calmodulin-binding proteins in the soluble fraction. These results show for the first time that beta2-glycoprotein I binds calmodulin and that beta2-glycoprotein I may in kidney be a membrane-associated protein. Immunohistochemical studies identified beta2-glycoprotein I in several parts of the cortex and the medulla of the kidney, including Bowman's capsula, the tubular lumen and the tubular epithelium, indicating that beta2-glycoprotein I, despite its relatively high molecular mass, is filtrated in the glomerulus and subsequently reabsorbed by the tubular epithelium. This is in agreement with beta2-glycoprotein I being a marker for renal tubular disease. | lld:pubmed |
| pubmed-article:9187240 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9187240 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187240 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9187240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187240 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9187240 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9187240 | pubmed:month | May | lld:pubmed |
| pubmed-article:9187240 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:9187240 | pubmed:author | pubmed-author:SchousboeII | lld:pubmed |
| pubmed-article:9187240 | pubmed:author | pubmed-author:ChristensenLL | lld:pubmed |
| pubmed-article:9187240 | pubmed:author | pubmed-author:KlaerkeD ADA | lld:pubmed |
| pubmed-article:9187240 | pubmed:author | pubmed-author:RøjkjaerRR | lld:pubmed |
| pubmed-article:9187240 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9187240 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:9187240 | pubmed:volume | 1339 | lld:pubmed |
| pubmed-article:9187240 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9187240 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9187240 | pubmed:pagination | 203-16 | lld:pubmed |
| pubmed-article:9187240 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:meshHeading | pubmed-meshheading:9187240-... | lld:pubmed |
| pubmed-article:9187240 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9187240 | pubmed:articleTitle | Identification of beta2-glycoprotein I as a membrane-associated protein in kidney: purification by calmodulin affinity chromatography. | lld:pubmed |
| pubmed-article:9187240 | pubmed:affiliation | Biomembrane Research Center, Department of Medical Physiology, The Panum Institute, University of Copenhagen, Copenhagen N, Denmark. | lld:pubmed |
| pubmed-article:9187240 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9187240 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9187240 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9187240 | lld:pubmed |
