| pubmed-article:7190147 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7190147 | lifeskim:mentions | umls-concept:C0205161 | lld:lifeskim |
| pubmed-article:7190147 | lifeskim:mentions | umls-concept:C0037628 | lld:lifeskim |
| pubmed-article:7190147 | lifeskim:mentions | umls-concept:C0039808 | lld:lifeskim |
| pubmed-article:7190147 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:7190147 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:7190147 | pubmed:dateCreated | 1980-9-23 | lld:pubmed |
| pubmed-article:7190147 | pubmed:abstractText | The thermodynamics of both normal and abnormal (disease-associated) protein solubility has been examined. It is shown that the atypical behavior of monoclonal cryoimmunoglobulins can be explained by the formation of one or a few additional electrostatic contacts or, less frequently, a larger number of van der Waals interactions in the protein-rich solid phase relative to normal immunoglobulin. It is hypothesized that cryoimmunoglobulins represent the outer edge of the solubility distribution of total serum immunoglobulin. | lld:pubmed |
| pubmed-article:7190147 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7190147 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7190147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7190147 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7190147 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7190147 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7190147 | pubmed:author | pubmed-author:RosenbergAA | lld:pubmed |
| pubmed-article:7190147 | pubmed:author | pubmed-author:LitmanG WGW | lld:pubmed |
| pubmed-article:7190147 | pubmed:author | pubmed-author:MiddaughC RCR | lld:pubmed |
| pubmed-article:7190147 | pubmed:author | pubmed-author:TiselW AWA | lld:pubmed |
| pubmed-article:7190147 | pubmed:author | pubmed-author:LawsonE QEQ | lld:pubmed |
| pubmed-article:7190147 | pubmed:author | pubmed-author:MoodD ADA | lld:pubmed |
| pubmed-article:7190147 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7190147 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:7190147 | pubmed:volume | 255 | lld:pubmed |
| pubmed-article:7190147 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7190147 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7190147 | pubmed:pagination | 6532-4 | lld:pubmed |
| pubmed-article:7190147 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:meshHeading | pubmed-meshheading:7190147-... | lld:pubmed |
| pubmed-article:7190147 | pubmed:year | 1980 | lld:pubmed |
| pubmed-article:7190147 | pubmed:articleTitle | Thermodynamic basis for the abnormal solubility of monoclonal cryoimmunoglobulins. | lld:pubmed |
| pubmed-article:7190147 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7190147 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7190147 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7190147 | lld:pubmed |
