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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1982-3-22
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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.
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pubmed:language |
fre
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aminopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Octoxynol,
http://linkedlifedata.com/resource/pubmed/chemical/Polyethylene Glycols,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/gamma-Glutamyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0009-8981
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
118
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
77-85
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6119171-Aminopeptidases,
pubmed-meshheading:6119171-Female,
pubmed-meshheading:6119171-Humans,
pubmed-meshheading:6119171-Isoenzymes,
pubmed-meshheading:6119171-Kidney Cortex,
pubmed-meshheading:6119171-Male,
pubmed-meshheading:6119171-Molecular Weight,
pubmed-meshheading:6119171-Octoxynol,
pubmed-meshheading:6119171-Polyethylene Glycols,
pubmed-meshheading:6119171-Solubility,
pubmed-meshheading:6119171-Trypsin,
pubmed-meshheading:6119171-Ultracentrifugation,
pubmed-meshheading:6119171-gamma-Glutamyltransferase
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pubmed:year |
1982
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pubmed:articleTitle |
[Urinary elimination of multiple forms of gamma-glutamyltranspeptidase and aminopeptidase (author's transl)].
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pubmed:publicationType |
Journal Article,
English Abstract,
Research Support, Non-U.S. Gov't
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