pubmed-article:6119171 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6119171 | lifeskim:mentions | umls-concept:C0341628 | lld:lifeskim |
pubmed-article:6119171 | lifeskim:mentions | umls-concept:C0221102 | lld:lifeskim |
pubmed-article:6119171 | lifeskim:mentions | umls-concept:C1524119 | lld:lifeskim |
pubmed-article:6119171 | lifeskim:mentions | umls-concept:C0002570 | lld:lifeskim |
pubmed-article:6119171 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
pubmed-article:6119171 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:6119171 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:6119171 | pubmed:dateCreated | 1982-3-22 | lld:pubmed |
pubmed-article:6119171 | pubmed:abstractText | Concentrated and dialyzed 24-h urines of healthy persons were separated by 105000 X g ultracentrifugation into a pellet (P105) and a supernatant (S105) fraction. Chromatography of the P105 fraction on Sepharose 4B and 2B revealed that gamma-glutamyltranspeptidase and aminopeptidase activities had a molecular mass of 20 X 10(5) to 40 X 10(6), whereas in the S105 fraction soluble gamma-glutamyltranspeptidase and aminopeptidase had 86000 and 160000, respectively. Triton X-100 solubilization was performed on the P105 fraction and on a human renal cortex 40000 X g pellet, used as a reference. All the activity was recovered in both cases in a single peak of detergent gamma-glutamyltranspeptidase and detergent aminopeptidase eluted by filtration on Ultrogel Ac A22. Apparent molecular mass of Triton X-100 solubilized urinary and renal enzymes were 250000 and 243000 for gamma-glutamyltranspeptidase, and 298000 for both aminopeptidases. Protease solubilized forms were obtained by trypsic digestion of detergent urinary and renal forms. Both gamma-glutamyltranspeptidases were found to have an apparent molecular mass of 86000 on Sephadex G 150, which is identical to the value found for the S105 urinary gamma-glutamyltranspeptidase. The aminopeptidases had 238000 and 232000, which is a higher value than the molecular mass of the S105 urinary aminopeptidase. This letter could be a degraded form of the renal aminopeptidase. These findings suggest that gamma-glutamyltranspeptidase and aminopeptidase in the P105 fraction are similar to native renal enzymes. Evaluation of the P105 fraction enzymatic activities may thus be useful in the diagnosis of tubular damage. | lld:pubmed |
pubmed-article:6119171 | pubmed:language | fre | lld:pubmed |
pubmed-article:6119171 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6119171 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:6119171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6119171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6119171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6119171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6119171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6119171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6119171 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6119171 | pubmed:month | Jan | lld:pubmed |
pubmed-article:6119171 | pubmed:issn | 0009-8981 | lld:pubmed |
pubmed-article:6119171 | pubmed:author | pubmed-author:LinderMM | lld:pubmed |
pubmed-article:6119171 | pubmed:author | pubmed-author:SudakaPP | lld:pubmed |
pubmed-article:6119171 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6119171 | pubmed:day | 5 | lld:pubmed |
pubmed-article:6119171 | pubmed:volume | 118 | lld:pubmed |
pubmed-article:6119171 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6119171 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6119171 | pubmed:pagination | 77-85 | lld:pubmed |
pubmed-article:6119171 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:6119171 | pubmed:year | 1982 | lld:pubmed |
pubmed-article:6119171 | pubmed:articleTitle | [Urinary elimination of multiple forms of gamma-glutamyltranspeptidase and aminopeptidase (author's transl)]. | lld:pubmed |
pubmed-article:6119171 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6119171 | pubmed:publicationType | English Abstract | lld:pubmed |
pubmed-article:6119171 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |